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Conserved domains on  [gi|1238238997|gb|PAM75587|]
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serine acetyltransferase [Bacillus subtilis]

Protein Classification

serine O-acetyltransferase( domain architecture ID 11437200)

serine O-acetyltransferase (SAT) catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetyl-L-serine

CATH:  2.160.10.10
EC:  2.3.1.30
Gene Ontology:  GO:0009001|GO:0006535
PubMed:  15500694|11747907|15581568
SCOP:  4001889

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 3-175 1.45e-115

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


:

Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 326.66  E-value: 1.45e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997   3 FRMLKEDIDTVFDQDPAARSYFEVILTYSGLHAIWAHRIAHALYKRKFYFLARLISQVSRFFTGIEIHPGATIGRRFFID 82
Cdd:COG1045     2 LKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFID 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  83 HGMGVVIGETCEIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVV 162
Cdd:COG1045    82 HGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVV 161

                         170
                  ....*....|...
gi 1238238997 163 GIPGRVVVQNGKK 175
Cdd:COG1045   162 GVPARIVKRKGSK 174
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 3-175 1.45e-115

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 326.66  E-value: 1.45e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997   3 FRMLKEDIDTVFDQDPAARSYFEVILTYSGLHAIWAHRIAHALYKRKFYFLARLISQVSRFFTGIEIHPGATIGRRFFID 82
Cdd:COG1045     2 LKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFID 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  83 HGMGVVIGETCEIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVV 162
Cdd:COG1045    82 HGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVV 161

                         170
                  ....*....|...
gi 1238238997 163 GIPGRVVVQNGKK 175
Cdd:COG1045   162 GVPARIVKRKGSK 174
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 6-167 4.31e-103

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 294.59  E-value: 4.31e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997   6 LKEDIDTVFDQDPAARSYFEVILTYSGLHAIWAHRIAHALYKRKFYFLARLISQVSRFFTGIEIHPGATIGRRFFIDHGM 85
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  86 GVVIGETCEIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIP 165
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 1238238997 166 GR 167
Cdd:TIGR01172 161 AR 162
cysE PRK11132
serine acetyltransferase; Provisional
 9-169 1.15e-59

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 188.37  E-value: 1.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997   9 DIDTVFDQDPAARSYFEVILTYSGLHAIWAHRIAHALYKRKFYFLA-RLISQVSRFFtGIEIHPGATIGRRFFIDHGMGV 87
Cdd:PRK11132   84 DIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAiYLQNQISVAF-QVDIHPAAKIGRGIMLDHATGI 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  88 VIGETCEIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGR 167
Cdd:PRK11132  163 VIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPAR 242


                  ..
gi 1238238997 168 VV 169
Cdd:PRK11132  243 IV 244
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 65-165 4.32e-56

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 173.40  E-value: 4.32e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  65 TGIEIHPGATIGRRFFIDHGMGVVIGETCEIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSK 144
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90       100
                  ....*....|....*....|.
gi 1238238997 145 IGAGSVVLHDVPDFSTVVGIP 165
Cdd:cd03354    81 IGANAVVTKDVPANSTVVGVP 101
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-36 2.68e-04

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants.and bacteria.


Pssm-ID: 198039 [Multi-domain]  Cd Length: 105  Bit Score: 39.06  E-value: 2.68e-04
                           10        20
                   ....*....|....*....|....*...
gi 1238238997    9 DIDTVFDQDPAARSYFEVILTYSGLHAI 36
Cdd:smart00971  76 DIQAVYDRDPACDRYLTPLLYFKGFHAL 103
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-36 1.28e-03

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants and bacteria.


Pssm-ID: 461909 [Multi-domain]  Cd Length: 104  Bit Score: 37.06  E-value: 1.28e-03
                          10        20
                  ....*....|....*....|....*...
gi 1238238997   9 DIDTVFDQDPAARSYFEVILTYSGLHAI 36
Cdd:pfam06426  76 DLQAVYERDPACDRYLTPLLYFKGFHAL 103
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 3-175 1.45e-115

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 326.66  E-value: 1.45e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997   3 FRMLKEDIDTVFDQDPAARSYFEVILTYSGLHAIWAHRIAHALYKRKFYFLARLISQVSRFFTGIEIHPGATIGRRFFID 82
Cdd:COG1045     2 LKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFID 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  83 HGMGVVIGETCEIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVV 162
Cdd:COG1045    82 HGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVV 161

                         170
                  ....*....|...
gi 1238238997 163 GIPGRVVVQNGKK 175
Cdd:COG1045   162 GVPARIVKRKGSK 174
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 6-167 4.31e-103

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 294.59  E-value: 4.31e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997   6 LKEDIDTVFDQDPAARSYFEVILTYSGLHAIWAHRIAHALYKRKFYFLARLISQVSRFFTGIEIHPGATIGRRFFIDHGM 85
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  86 GVVIGETCEIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIP 165
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 1238238997 166 GR 167
Cdd:TIGR01172 161 AR 162
cysE PRK11132
serine acetyltransferase; Provisional
 9-169 1.15e-59

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 188.37  E-value: 1.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997   9 DIDTVFDQDPAARSYFEVILTYSGLHAIWAHRIAHALYKRKFYFLA-RLISQVSRFFtGIEIHPGATIGRRFFIDHGMGV 87
Cdd:PRK11132   84 DIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAiYLQNQISVAF-QVDIHPAAKIGRGIMLDHATGI 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  88 VIGETCEIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGR 167
Cdd:PRK11132  163 VIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPAR 242


                  ..
gi 1238238997 168 VV 169
Cdd:PRK11132  243 IV 244
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 65-165 4.32e-56

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 173.40  E-value: 4.32e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  65 TGIEIHPGATIGRRFFIDHGMGVVIGETCEIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSK 144
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90       100
                  ....*....|....*....|.
gi 1238238997 145 IGAGSVVLHDVPDFSTVVGIP 165
Cdd:cd03354    81 IGANAVVTKDVPANSTVVGVP 101
PLN02357 PLN02357
serine acetyltransferase
 4-169 9.96e-55

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 178.54  E-value: 9.96e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997   4 RMLKEDIDTVFDQDPAARSYFEVILTYSGLHAIWAHRIAHALYKRKFYFLARLI-SQVSRFFtGIEIHPGATIGRRFFID 82
Cdd:PLN02357  164 ESVKQDLRAVKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILALLIqNRVSEAF-AVDIHPGAKIGQGILLD 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  83 HGMGVVIGETCEIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVV 162
Cdd:PLN02357  243 HATGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAV 322


                  ....*..
gi 1238238997 163 GIPGRVV 169
Cdd:PLN02357  323 GNPARLI 329
PLN02739 PLN02739
serine acetyltransferase
 6-169 1.16e-52

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 172.91  E-value: 1.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997   6 LKEDIDTVFDQDPAARSYFEVILTYSGLHAIWAHRIAHALYK--RKFYFLArLISQVSRFFtGIEIHPGATIGRRFFIDH 83
Cdd:PLN02739  145 IRLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKqgRKLLALA-LQSRVSEVF-GIDIHPAARIGKGILLDH 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  84 GMGVVIGETCEIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVG 163
Cdd:PLN02739  223 GTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAG 302


                  ....*.
gi 1238238997 164 IPGRVV 169
Cdd:PLN02739  303 NPAKLI 308
PLN02694 PLN02694
serine O-acetyltransferase
 16-191 3.99e-52

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 169.82  E-value: 3.99e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  16 QDPAARSYFEVILTYSGLHAIWAHRIAHALY--KRKFYFLArLISQVSRFFtGIEIHPGATIGRRFFIDHGMGVVIGETC 93
Cdd:PLN02694  110 RDPACVSFSHCLLNYKGFLACQAHRVAHKLWtqSRRPLALA-LHSRISDVF-AVDIHPAAKIGKGILFDHATGVVIGETA 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  94 EIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRVVvqNG 173
Cdd:PLN02694  188 VIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV--GG 265

                         170
                  ....*....|....*...
gi 1238238997 174 KKvrRDLNHQDLPDPVAD 191
Cdd:PLN02694  266 KE--KPAKHEECPGESMD 281
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
47-169 2.34e-23

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 91.09  E-value: 2.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  47 KRKFYFLARlISQVSRFFTGIEIHPG-ATIGRRFFIDHGMGVVIGETCEIGNNVTVFQGVTLGGTG--------KEKGKR 117
Cdd:COG0110     2 KLLLLFGAR-IGDGVVIGPGVRIYGGnITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNhpiddpatFPLRTG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1238238997 118 HPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRVV 169
Cdd:COG0110    81 PVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVI 132
PRK10191 PRK10191
putative acyl transferase; Provisional
 36-170 2.65e-21

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 85.71  E-value: 2.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  36 IWAHRIAH--ALYKRK----------FYFLARLISQVsrfFTGIEIHPGATIGRRFFIDHGMGVVIGETCEIGNNVTVFQ 103
Cdd:PRK10191    2 VLAYRVAHfcSVWRKKnvlnnlwaapLLVLYRIITEC---FFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRH 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238238997 104 GVTLGGTGKEKgKRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRVVV 170
Cdd:PRK10191   79 GVTIGNRGADN-MACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARVKV 144
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 69-165 6.16e-20

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 83.70  E-value: 6.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  69 IHPGATIGRRFFIDHGmgVVIGETCEIGNNVTVFQGVTLGGtgkekgkrHPTIKDDALIATGAKVLGSITVGEGSKIGAG 148
Cdd:TIGR03570 114 INPDVRIGDNVIINTG--AIVEHDCVIGDFVHIAPGVTLSG--------GVVIGEGVFIGAGATIIQGVTIGAGAIVGAG 183

                          90
                  ....*....|....*..
gi 1238238997 149 SVVLHDVPDFSTVVGIP 165
Cdd:TIGR03570 184 AVVTKDIPDGGVVVGVP 200
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 66-169 1.25e-19

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 80.19  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  66 GIEIHPGATIGRRFFIDHGMGVVIGETCEIGNNVTVF--------------QGVTLGGTgkekgkrhpTIKDDALIATGA 131
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYdhnhdiddperpieQGVTSAPI---------VIGDDVWIGANV 71

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1238238997 132 KVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRVV 169
Cdd:cd04647    72 VILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 75-169 1.61e-19

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 80.24  E-value: 1.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  75 IGRRFFIDHGmgVVIGETCEIGNNVTVFQGVTLG------------------GTGKEKGK-RHPTIKDDALIATGAKVLG 135
Cdd:cd03358     7 IGTNVFIEND--VKIGDNVKIQSNVSIYEGVTIEddvfigpnvvftndlyprSKIYRKWElKGTTVKRGASIGANATILP 84

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1238238997 136 SITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRVV 169
Cdd:cd03358    85 GVTIGEYALVGAGAVVTKDVPPYALVVGNPARII 118
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 39-165 1.00e-18

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 80.22  E-value: 1.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  39 HRIAHALYKRKfYFLARLISQVSRFFTGIEIHPG------------ATIGRRFFIDHGmgVVIGETCEIGNNVTVFQGVT 106
Cdd:cd03360    70 RKLAEKLLAAG-YRFATLIHPSAVVSPSAVIGEGcvimagavinpdARIGDNVIINTG--AVIGHDCVIGDFVHIAPGVV 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1238238997 107 LGGtgkekgkrHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIP 165
Cdd:cd03360   147 LSG--------GVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 74-169 2.15e-18

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 78.62  E-value: 2.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  74 TIGRRFFIDHGM------GVVIGETCEIGNNVTVFQG-----VTLGGTGKEKGKrhP-TIKDDALIATGAKVLGSITVGE 141
Cdd:cd03357    64 HIGDNFYANFNCtildvaPVTIGDNVLIGPNVQIYTAghpldPEERNRGLEYAK--PiTIGDNVWIGGGVIILPGVTIGD 141

                          90       100
                  ....*....|....*....|....*...
gi 1238238997 142 GSKIGAGSVVLHDVPDFSTVVGIPGRVV 169
Cdd:cd03357   142 NSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 73-152 5.94e-15

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 67.27  E-value: 5.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  73 ATIGRRFFIDHGmgVVIGETCEIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVL 152
Cdd:cd00208     1 VFIGEGVKIHPK--AVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 67-169 9.50e-15

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 68.34  E-value: 9.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  67 IEIHPGATIGRRFFIDHGMGVVIGETCEIGNNVTV---------------FQGVTLGGTGKEKGKRHP-----TIKDDAL 126
Cdd:cd03349     2 ISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIglggnhptdwvstypFYIFGGEWEDDAKFDDWPskgdvIIGNDVW 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1238238997 127 IATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRVV 169
Cdd:cd03349    82 IGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVI 124
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 86-185 2.06e-12

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 62.74  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  86 GVVI----GETCEIGNNVTVFQGVTLGGtgkekgkrhPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHD--VPDFS 159
Cdd:COG0663    61 GVVLhvdpGYPLTIGDDVTIGHGAILHG---------CTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGkvVPPGS 131

                          90       100
                  ....*....|....*....|....*.
gi 1238238997 160 TVVGIPGRVVvqngkkvrRDLNHQDL 185
Cdd:COG0663   132 LVVGSPAKVV--------RELTEEEI 149
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 63-184 4.53e-12

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 62.71  E-value: 4.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  63 FFTGIEIHpgatIGRRFFIDHGMGVVIGETCEIGNNVTVFQGVTLGGTG-------KEKGKRHP---TIKDDALIATGAK 132
Cdd:PRK09527   70 FSYGSNIH----IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGhpvhhelRKNGEMYSfpiTIGNNVWIGSHVV 145

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1238238997 133 VLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRVVvqngkkvrRDLNHQD 184
Cdd:PRK09527  146 INPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVI--------REINDRD 189
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 74-169 6.09e-11

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 58.58  E-value: 6.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  74 TIGRRFFI-DhgmGVVI----GETCEIGNNVTVFQGVTLGGTgkekgkrhpTIKDDALIATGAKVLGSITVGEGSKIGAG 148
Cdd:cd04645    40 RIGERTNIqD---GSVLhvdpGYPTIIGDNVTVGHGAVLHGC---------TIGDNCLIGMGAIILDGAVIGKGSIVAAG 107

                          90       100
                  ....*....|....*....|...
gi 1238238997 149 SVVLHD--VPDFSTVVGIPGRVV 169
Cdd:cd04645   108 SLVPPGkvIPPGSLVAGSPAKVV 130
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 67-169 1.95e-10

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 56.07  E-value: 1.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  67 IEIHPGATIGRRFFIDHgMGVVigetcEIGNNVTVFQGVTL-GGTGKEKGKRHP------TIKDDALIATGAKVLGSITV 139
Cdd:cd05825     4 LTIGDNSWIGEGVWIYN-LAPV-----TIGSDACISQGAYLcTGSHDYRSPAFPlitapiVIGDGAWVAAEAFVGPGVTI 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1238238997 140 GEGSKIGAGSVVLHDVPDFSTVVGIPGRVV 169
Cdd:cd05825    78 GEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 66-173 9.95e-10

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 54.69  E-value: 9.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  66 GIEIHPGATIGRRFFIDhgMGVVIGETCEIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSKI 145
Cdd:cd03350    25 PSYVNIGAYVDEGTMVD--SWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKGAVL 102

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1238238997 146 GAGSVVLHDVPDFSTVVG------IPGRVVVQNG 173
Cdd:cd03350   103 AAGVVLTQSTPIYDRETGeiyygrVPPGSVVVAG 136
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 34-173 1.91e-09

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 56.30  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  34 HAIWAhRIAHALYKRKfyflarlisqVSRFFTGIE----IHPGATIGRRFFIDHGmgVVIGETCEIGNNVTVFQGVTLGg 109
Cdd:PRK00892   81 YLAFA-RLAQLFDPPA----------TPSPAAGIHpsavIDPSAKIGEGVSIGPN--AVIGAGVVIGDGVVIGAGAVIG- 146

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997 110 tgkekgkRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHD----VPDFSTVVGIP--GRVVVQNG 173
Cdd:PRK00892  147 -------DGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIGSDgfgfANDRGGWVKIPqlGRVIIGDD 209
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 50-173 7.28e-09

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 54.64  E-value: 7.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  50 FYFLARLISQVSRFFTGIE----IHPGATIGRRFFIDHGmgVVIGETCEIGNNVTVFQGVTLGgtgkekgkRHPTIKDDA 125
Cdd:COG1044    82 FAKLLQLFYPPPAPAPGIHpsavIDPSAKIGEGVSIGPF--AVIGAGVVIGDGVVIGPGVVIG--------DGVVIGDDC 151

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238238997 126 LIATGAkvlgsiTVGEGSKIGAGsVVLHDvpdfSTVVG----------------IP--GRVVVQNG 173
Cdd:COG1044   152 VLHPNV------TIYERCVIGDR-VIIHS----GAVIGadgfgfapdedggwvkIPqlGRVVIGDD 206
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 93-169 6.21e-08

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 51.56  E-value: 6.21e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238238997  93 CEIGNNVTVFQGVTLGGtgkekgkrHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRVV 169
Cdd:COG1043   123 CVVGNNVILANNATLAG--------HVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLR 191
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 69-165 1.71e-07

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 49.71  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  69 IHPGATIG-----------RRFFIDHGMGVVIGETCEIGNNVTVFQGvTLGGT--GK--------------EKGKR---- 117
Cdd:cd03352    64 IHSGAVIGsdgfgfapdggGWVKIPQLGGVIIGDDVEIGANTTIDRG-ALGDTviGDgtkidnlvqiahnvRIGENclia 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1238238997 118 -------HPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIP 165
Cdd:cd03352   143 aqvgiagSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTP 197
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 89-169 1.93e-07

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 50.12  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  89 IGETCEIGNNVTVFQGVTLGGtgkekgkrHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRV 168
Cdd:cd03351   117 VAHDCVIGNNVILANNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARL 188


                  .
gi 1238238997 169 V 169
Cdd:cd03351   189 R 189
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 68-168 2.33e-07

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 50.41  E-value: 2.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  68 EIHPGATIG-----RrffidhgMGVVIGETCEIGNNV----------------------TVFQGVTLG-GT------GKE 113
Cdd:COG1207   319 VVGAGATVGpfarlR-------PGTVLGEGVKIGNFVevknstigegskvnhlsyigdaEIGEGVNIGaGTitcnydGVN 391

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238238997 114 KgkrHPT-IKDDALIatgakvlGS-------ITVGEGSKIGAGSVVLHDVPDFSTVVG------IPGRV 168
Cdd:COG1207   392 K---HRTvIGDGAFI-------GSntnlvapVTIGDGATIGAGSTITKDVPAGALAIArarqrnIEGWV 450
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 82-171 2.33e-07

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 48.72  E-value: 2.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  82 DHGMGVVIGETCEIGNNVTVfQGVTLGgtgkekgkrhptikDDALIATGAKVLGSITVGEGSKIGAGSVVLH--DVPDFS 159
Cdd:cd04650    57 DHGYPTEIGDYVTIGHNAVV-HGAKVG--------------NYVIVGMGAILLNGAKIGDHVIIGAGAVVTPgkEIPDYS 121

                          90
                  ....*....|..
gi 1238238997 160 TVVGIPGRVVVQ 171
Cdd:cd04650   122 LVLGVPAKVVRK 133
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
89-168 2.39e-07

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 49.71  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  89 IGETCEIGNNVTVFQGVTLGGtgkekgkrHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRV 168
Cdd:PRK05289  120 VAHDCVVGNHVILANNATLAG--------HVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARL 191
PRK10502 PRK10502
putative acyl transferase; Provisional
 66-169 3.98e-07

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 48.41  E-value: 3.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  66 GIEIHPGA--------TIGrrffiDH---GMGVVIG--ETCEIGNNVTVFQGVTLGGTGKEKGKRH------P-TIKDDA 125
Cdd:PRK10502   57 GVVIRPSVritypwklTIG-----DYawiGDDVWLYnlGEITIGAHCVISQKSYLCTGSHDYSDPHfdlntaPiVIGEGC 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1238238997 126 LIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRVV 169
Cdd:PRK10502  132 WLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPI 175
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 95-178 4.57e-07

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 49.38  E-value: 4.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  95 IGNNVTVFQG-VTLGGTGKekgKRHPT-IKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRVVVQN 172
Cdd:PRK14357  361 VGKNVNIGAGtITCNYDGK---KKNPTfIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKEG 437


                  ....*.
gi 1238238997 173 GKKVRR 178
Cdd:PRK14357  438 WVLKKR 443
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 72-165 1.04e-06

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 48.59  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  72 GATIGRRFFIDhgmGVVIGET--CEIGNNVTVFQGVTLGGTGKEKG---KRHPTIKDDALIATGAKVLGSITVGEGSKIG 146
Cdd:TIGR02353 597 GVKIGRGVYID---GTDLTERdlVTIGDDSTLNEGSVIQTHLFEDRvmkSDTVTIGDGATLGPGAIVLYGVVMGEGSVLG 673

                          90       100
                  ....*....|....*....|.
gi 1238238997 147 AGSVVL--HDVPDFSTVVGIP 165
Cdd:TIGR02353 674 PDSLVMkgEEVPAHTRWRGNP 694
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 31-179 1.04e-06

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 48.59  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  31 SGLHAIWAhriahaLYKRKFYFLARLI-SQVSRFFTGIEIHP------GATIGRRFFIdHGMGVVIGETCEIGNNVTVFQ 103
Cdd:TIGR02353  70 PGTYPIWG------STYLRFWTVKRLVdAAPTVLLSGSPLYSlylralGAKIGKGVDI-GSLPPVCTDLLTIGAGTIVRK 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997 104 GVTLGGTGKEKGKRHP---TIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHD--VPDFSTVVGIPGRVVVQNGKKVRR 178
Cdd:TIGR02353 143 EVMLLGYRAERGRLHTgpvTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGqsIPDGERWHGSPAQKTGADYRKVQP 222


                  .
gi 1238238997 179 D 179
Cdd:TIGR02353 223 A 223
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 64-163 6.43e-06

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 45.10  E-value: 6.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  64 FTGIEIHPGATIG-----RrffidhgMGVVIGETCEIGNNV----------------------TVFQGVTLG-GT----- 110
Cdd:cd03353    65 IEGAVIGNGATVGpfahlR-------PGTVLGEGVHIGNFVeikkstigegskanhlsylgdaEIGEGVNIGaGTitcny 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1238238997 111 -GKEKgkrHPT-IKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVG 163
Cdd:cd03353   138 dGVNK---HRTvIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIA 189
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 73-172 1.16e-05

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 44.32  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  73 ATIGRRFFIDHGmgVVIGETCEIGNNVTVFQGVTLGgtgkekgkRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVL 152
Cdd:cd03352     2 AKIGENVSIGPN--AVIGEGVVIGDGVVIGPGVVIG--------DGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIG 71

                          90       100
                  ....*....|....*....|....*.
gi 1238238997 153 HD----VPDFSTVVGIP--GRVVVQN 172
Cdd:cd03352    72 SDgfgfAPDGGGWVKIPqlGGVIIGD 97
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 69-199 1.50e-05

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 44.62  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  69 IHPGATIGRRFFIDHGmgVVIGETCEIGNNVTVFQGVTLGGTG-----KEKGKRHP-------TIKDD------------ 124
Cdd:COG1044   141 IGDGVVIGDDCVLHPN--VTIYERCVIGDRVIIHSGAVIGADGfgfapDEDGGWVKipqlgrvVIGDDveiganttidrg 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997 125 AL----IATGAK------------------------------------------VLGSITVGEGSKIGAGSVVLHDVPDF 158
Cdd:COG1044   219 ALgdtvIGDGTKidnlvqiahnvrigehtaiaaqvgiagstkigdnvviggqvgIAGHLTIGDGVIIGAQSGVTKSIPEG 298

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1238238997 159 STVVGIPG---RVVVQNGKKVRRdlnhqdLPDpVADRFKSLEQQ 199
Cdd:COG1044   299 GVYSGSPAqphREWLRNAAALRR------LPE-LAKRLKELEKK 335
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 72-169 1.53e-05

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 44.03  E-value: 1.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  72 GATIGRRFFIDHGMGVVIGET------------CE--IGNNVTVFQGV-----------TLGGTGKEKGKrhP-TIKDDA 125
Cdd:PRK10092   59 EAYIEPTFRCDYGYNIFLGNNfyanfdcvmldvCPirIGDNCMLAPGVhiytathpldpVARNSGAELGK--PvTIGNNV 136

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1238238997 126 LIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRVV 169
Cdd:PRK10092  137 WIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARII 180
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 93-157 1.73e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 44.71  E-value: 1.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238238997  93 CEIGNNVTVFQG-VTLGGTGKEKgkrHPT-IKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPD 157
Cdd:PRK14356  374 AEIGAGANIGAGtITCNYDGVNK---HRTvIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPD 437
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 75-155 1.83e-05

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 41.79  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  75 IGRRFFIDHG---MGVVIGETCEIGNNVTVfqgvtlggtgkekgkRHPTIKDDALIATGAKVLGSI-----TVGEGSKIG 146
Cdd:cd05787     2 IGRGTSIGEGttiKNSVIGRNCKIGKNVVI---------------DNSYIWDDVTIEDGCTIHHSIvadgaVIGKGCTIP 66


                  ....*....
gi 1238238997 147 AGSVVLHDV 155
Cdd:cd05787    67 PGSLISFGV 75
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 73-174 2.28e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 44.54  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  73 ATIGRRFFIDHGMGV---VIGETCEIG-NNVTV-FQGVTlggtgkekgKRHPTIKDDALIATGAKVLGSITVGEGSKIGA 147
Cdd:PRK14352  358 ATIGRGTKVPHLTYVgdaDIGEHSNIGaSSVFVnYDGVN---------KHRTTIGSHVRTGSDTMFVAPVTVGDGAYTGA 428

                          90       100
                  ....*....|....*....|....*..
gi 1238238997 148 GSVVLHDVPdfstvvgiPGRVVVQNGK 174
Cdd:PRK14352  429 GTVIREDVP--------PGALAVSEGP 447
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-175 4.77e-05

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 43.38  E-value: 4.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  87 VVIGETCEIGNNV----------------------TVFQGVTLG-GT------GKEKgkrHPTIKDDAlIATGAK-VL-G 135
Cdd:PRK14360  332 AQIGSNCRIGNFVeikksqlgegskvnhlsyigdaTLGEQVNIGaGTitanydGVKK---HRTVIGDR-SKTGANsVLvA 407

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1238238997 136 SITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRVVVQNGKK 175
Cdd:PRK14360  408 PITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIKENWKK 447
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 79-178 8.09e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 42.32  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  79 FFIDHgmgVVIGETCEIGNNVTVFQGVTLGGtgkekgkrHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDF 158
Cdd:PRK12461  109 LLMAY---SHVAHDCQIGNNVILVNGALLAG--------HVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPPY 177

                          90       100
                  ....*....|....*....|
gi 1238238997 159 STVVGIPGRVVVQNGKKVRR 178
Cdd:PRK12461  178 CMMAGHPTNVHGLNAVGLRR 197
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 69-159 1.09e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 42.51  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  69 IHPGATIGRrffidhgmGVVIGETCE-----IGNN-----------VTVFQGVTLG-GT------GKEKgkrHPT-IKDD 124
Cdd:PRK14354  331 LRPGSVIGE--------EVKIGNFVEikkstIGEGtkvshltyigdAEVGENVNIGcGTitvnydGKNK---FKTiIGDN 399

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1238238997 125 ALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFS 159
Cdd:PRK14354  400 AFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDA 434
PLN02296 PLN02296
carbonate dehydratase
 95-167 1.77e-04

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 41.26  E-value: 1.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238238997  95 IGNNVTVFQGVTLGGTgkekgkrhpTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHD--VPDFSTVVGIPGR 167
Cdd:PLN02296  122 IGDNVTIGHSAVLHGC---------TVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAK 187
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-36 2.68e-04

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants.and bacteria.


Pssm-ID: 198039 [Multi-domain]  Cd Length: 105  Bit Score: 39.06  E-value: 2.68e-04
                           10        20
                   ....*....|....*....|....*...
gi 1238238997    9 DIDTVFDQDPAARSYFEVILTYSGLHAI 36
Cdd:smart00971  76 DIQAVYDRDPACDRYLTPLLYFKGFHAL 103
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 117-163 6.07e-04

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 39.24  E-value: 6.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238238997 117 RHPTIKDDALIATGAKVLGSITVGEGS---------------KIGAGS-----VVLHDVPDFSTVVG 163
Cdd:COG0663     9 KTPQIHPSAFVAPTAVVIGDVTIGEDVsvwpgavlrgdvgpiRIGEGSniqdgVVLHVDPGYPLTIG 75
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 87-169 7.38e-04

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 39.09  E-value: 7.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  87 VVIGETCEIGNNVTVFQGVTlggtgkekgkrhptikddaliatgakvlgsitVGEGSKIGAGSVVLHDVPDFSTVVGIPG 166
Cdd:PRK09677  131 VVIGQRVWIGENVTILPGVS--------------------------------IGNGCIVGANSVVTKSIPENTVIAGNPA 178


                  ...
gi 1238238997 167 RVV 169
Cdd:PRK09677  179 KII 181
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 64-169 1.01e-03

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 38.12  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  64 FTGIEIHPGATIGRRFFIdHGMgvvIGETCEIGNNVTVFQGVTLGGTgkekgkrhpTIKDDALIATGAKVLGSITVGEGS 143
Cdd:cd04745    37 FGRIVIRDGANVQDNCVI-HGF---PGQDTVLEENGHIGHGAILHGC---------TIGRNALVGMNAVVMDGAVIGEES 103

                          90       100
                  ....*....|....*....|....*...
gi 1238238997 144 KIGAGSVVL--HDVPDFSTVVGIPGRVV 169
Cdd:cd04745   104 IVGAMAFVKagTVIPPRSLIAGSPAKVI 131
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 94-157 1.18e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 39.24  E-value: 1.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238238997  94 EIGNNVTVFQGV-TLGGTGKEKGKRHptIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPD 157
Cdd:PRK09451  371 EIGDNVNIGAGTiTCNYDGANKFKTI--IGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAE 433
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-36 1.28e-03

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants and bacteria.


Pssm-ID: 461909 [Multi-domain]  Cd Length: 104  Bit Score: 37.06  E-value: 1.28e-03
                          10        20
                  ....*....|....*....|....*...
gi 1238238997   9 DIDTVFDQDPAARSYFEVILTYSGLHAI 36
Cdd:pfam06426  76 DLQAVYERDPACDRYLTPLLYFKGFHAL 103
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 69-151 1.76e-03

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 37.78  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  69 IHPGATIGRRFFIDHGM----GVVIGETCEIGNNVtvfqgvtlggtgkekgkrhpTIKdDALIATGAKVLGSiTVGEGSK 144
Cdd:cd03353    12 IDGDVEIGVDVVIDPGVilegKTVIGEDCVIGPNC--------------------VIK-DSTIGDGVVIKAS-SVIEGAV 69


                  ....*..
gi 1238238997 145 IGAGSVV 151
Cdd:cd03353    70 IGNGATV 76
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 69-177 2.15e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.08  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  69 IHPGATIGRrffidhgmGVVIGETCEIGNNVTvfqgvtlggtgkekgkrhptIKDDALIATGAKVLGSITVGEGSKIGAG 148
Cdd:PRK12461    8 IDPSAKLGS--------GVEIGPFAVIGANVE--------------------IGDGTWIGPHAVILGPTRIGKNNKIHQG 59

                          90       100
                  ....*....|....*....|....*....
gi 1238238997 149 SVVLHDVPDFsTVVGIPGRVVVQNGKKVR 177
Cdd:PRK12461   60 AVVGDEPQDF-TYKGEESRLEIGDRNVIR 87
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 69-203 2.38e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.20  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  69 IHPGATIGRRFF-----------IDHGMGVVIGETCEIGNNVTVFQGvTLGGTGKEKG-K--------------RH---- 118
Cdd:PRK00892  175 IHSGAVIGSDGFgfandrggwvkIPQLGRVIIGDDVEIGANTTIDRG-ALDDTVIGEGvKidnlvqiahnvvigRHtaia 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997 119 --------PTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVV-GIPgrvvVQNGKKVRRDLNH-QDLPDp 188
Cdd:PRK00892  254 aqvgiagsTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSsGIP----AQPNKEWLRTAARlRRLDE- 328

                         170
                  ....*....|....*
gi 1238238997 189 VADRFKSLEQQILEL 203
Cdd:PRK00892  329 LRKRLKALEKKVEQL 343
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 69-151 2.77e-03

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 38.08  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  69 IHPGATIGRRFFIDHGmgVVIGETCEIGNNVTVFQGVTLggtgkekgkrhptikDDALIATGAKVLGSitVGEGSKIGAG 148
Cdd:COG1207   263 IDGDVEIGRDVVIDPN--VILEGKTVIGEGVVIGPNCTL---------------KDSTIGDGVVIKYS--VIEDAVVGAG 323


                  ...
gi 1238238997 149 SVV 151
Cdd:COG1207   324 ATV 326
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 69-147 2.97e-03

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 35.30  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  69 IHPGATIGRRFFIDHgmgVVIGETCEIGNNVTVFQGVTLGGTGKEKGK--RHPTIKDDALIATGAKVLGSITVGEGSKIG 146
Cdd:cd03356     2 IGESTVIGENAIIKN---SVIGDNVRIGDGVTITNSILMDNVTIGANSviVDSIIGDNAVIGENVRVVNLCIIGDDVVVE 78


                  .
gi 1238238997 147 A 147
Cdd:cd03356    79 D 79
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 69-145 2.99e-03

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.81  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  69 IHPGATIGRRFFIdhGMGVVIGETCEIGNNVTVFQGVTLGGTG----KEKGKRHP-------TIKDDALIatGAK----- 132
Cdd:PRK00892  145 IGDGVKIGADCRL--HANVTIYHAVRIGNRVIIHSGAVIGSDGfgfaNDRGGWVKipqlgrvIIGDDVEI--GANttidr 220

                          90
                  ....*....|....
gi 1238238997 133 -VLGSITVGEGSKI 145
Cdd:PRK00892  221 gALDDTVIGEGVKI 234
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 116-163 3.72e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 37.53  E-value: 3.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1238238997 116 KRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVG 163
Cdd:PRK14353  378 KHRTEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALG 425
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 84-174 3.76e-03

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 37.40  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238238997  84 GMGVVIGETCEIGNnvtvfqGVTLGGTgKEKGKRHPT-IKDDALIATGAKVLGSITVGEGSKIGAGsVVL---------- 152
Cdd:COG2171   142 GSCAQIGKNVHLSG------GAGIGGV-LEPLQAAPViIEDNCFIGARSGVVEGVIVGEGAVLGAG-VYLtastkiydrv 213

                          90       100
                  ....*....|....*....|....*...
gi 1238238997 153 ------HDVPDFSTVVgiPGRVVVQNGK 174
Cdd:COG2171   214 tgevyyGRVPAGSVVV--PGSLPGKDGD 239
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 94-156 4.21e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.42  E-value: 4.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238238997  94 EIGNNVTVFQG-VTLGGTGKekgKRHPT-IKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVP 156
Cdd:PRK14355  374 TIGRNVNIGCGtITCNYDGV---KKHRTvIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVP 435
PLN02296 PLN02296
carbonate dehydratase
 119-155 4.67e-03

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 37.03  E-value: 4.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1238238997 119 PTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDV 155
Cdd:PLN02296   53 PVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDV 89
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
118-147 9.83e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 32.69  E-value: 9.83e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1238238997 118 HPTIKDDALIATGAKVLGSITVGEGSKIGA 147
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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