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Conserved domains on  [gi|389886429|emb|CCH23094|]
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alanine-anticapsin ligase, partial [Bacillus subtilis]

Protein Classification

acetyl-CoA carboxylase biotin carboxylase subunit family protein( domain architecture ID 11418417)

acetyl-CoA carboxylase biotin carboxylase subunit family protein similar to Bacillus subtilis alanine--anticapsin ligase that is part of the bacABCDEFG operon responsible for the biosynthesis of bacilysin, an irreversible inactivator of the glutaminase domain of glucosamine synthetase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 67-232 2.17e-34

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


:

Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 123.44  E-value: 2.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  67 EEVVEQIVKVAEMFGVDAITTNNELFIAPMAKACERLGLRGAGVQAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFR 146
Cdd:COG0439    3 DAIIAAAAELARETGIDAVLSESEFAVETAAELAEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEAL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429 147 AALEEIGTPLILKPTYLASSIGVTLITDTETAEAEFNRVndylksINVPKAVTFEAPFIAEEFLQGeygdwyqtegysDY 226
Cdd:COG0439   83 AFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEA------RAEAKAGSPNGEVLVEEFLEG------------RE 144


                 ....*.
gi 389886429 227 ISIEGI 232
Cdd:COG0439  145 YSVEGL 150
 
Name Accession Description Interval E-value
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 67-232 2.17e-34

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 123.44  E-value: 2.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  67 EEVVEQIVKVAEMFGVDAITTNNELFIAPMAKACERLGLRGAGVQAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFR 146
Cdd:COG0439    3 DAIIAAAAELARETGIDAVLSESEFAVETAAELAEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEAL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429 147 AALEEIGTPLILKPTYLASSIGVTLITDTETAEAEFNRVndylksINVPKAVTFEAPFIAEEFLQGeygdwyqtegysDY 226
Cdd:COG0439   83 AFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEA------RAEAKAGSPNGEVLVEEFLEG------------RE 144


                 ....*.
gi 389886429 227 ISIEGI 232
Cdd:COG0439  145 YSVEGL 150
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 76-187 6.26e-10

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 58.71  E-value: 6.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  76 VAEMFGVDAITTNNELFIAPMAKACERLGLRGAGVQAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGTP 155
Cdd:PRK02186  65 VSSLDGVAGIMSSSEYFIEVASEVARRLGLPAANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYP 144

                         90       100       110
                 ....*....|....*....|....*....|..
gi 389886429 156 LILKPTYLASSIGVTLITDTETAEAEFNRVND 187
Cdd:PRK02186 145 VVVKPRMGSGSVGVRLCASVAEAAAHCAALRR 176
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 37-212 3.03e-06

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 47.69  E-value: 3.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429    37 IKDKDYFKSLAdFEHPDSIYwaheDHDKPEEEVVEqivkvaemFGvdAITTNNelfiapMAKACERLGLR--GAGVQAAE 114
Cdd:TIGR01369  607 TSDRLYFEPLT-FEDVMNII----ELEKPEGVIVQ--------FG--GQTPLN------LAKALEEAGVPilGTSPESID 665

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429   115 NARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGTPLILKPTYLASSIGVTLITDTETaeaefnrVNDYLKSINv 194
Cdd:TIGR01369  666 RAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEE-------LRRYLEEAV- 737

                          170
                   ....*....|....*...
gi 389886429   195 pkAVTFEAPFIAEEFLQG 212
Cdd:TIGR01369  738 --AVSPEHPVLIDKYLED 753
ATP-grasp_4 pfam13535
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 152-213 5.41e-05

ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 316093 [Multi-domain]  Cd Length: 160  Bit Score: 42.27  E-value: 5.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 389886429  152 IGTPLILKPTYLASSIGVTLITDTETAEAEFNRVNDYLKSINV--PKAVTFEAPFIAEEFLQGE 213
Cdd:pfam13535   1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEIEQWKEmyPEAVVDGGSFLVEEYIEGE 64
 
Name Accession Description Interval E-value
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 67-232 2.17e-34

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 123.44  E-value: 2.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  67 EEVVEQIVKVAEMFGVDAITTNNELFIAPMAKACERLGLRGAGVQAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFR 146
Cdd:COG0439    3 DAIIAAAAELARETGIDAVLSESEFAVETAAELAEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEAL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429 147 AALEEIGTPLILKPTYLASSIGVTLITDTETAEAEFNRVndylksINVPKAVTFEAPFIAEEFLQGeygdwyqtegysDY 226
Cdd:COG0439   83 AFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEA------RAEAKAGSPNGEVLVEEFLEG------------RE 144


                 ....*.
gi 389886429 227 ISIEGI 232
Cdd:COG0439  145 YSVEGL 150
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 76-187 6.26e-10

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 58.71  E-value: 6.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  76 VAEMFGVDAITTNNELFIAPMAKACERLGLRGAGVQAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGTP 155
Cdd:PRK02186  65 VSSLDGVAGIMSSSEYFIEVASEVARRLGLPAANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYP 144

                         90       100       110
                 ....*....|....*....|....*....|..
gi 389886429 156 LILKPTYLASSIGVTLITDTETAEAEFNRVND 187
Cdd:PRK02186 145 VVVKPRMGSGSVGVRLCASVAEAAAHCAALRR 176
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
 100-212 2.44e-09

D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440794 [Multi-domain]  Cd Length: 303  Bit Score: 56.27  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429 100 CERLGLR--GAGVQAAENARDKNKMRDAFNKAGVKSIKNKRVT--TLEDFRAALEEIGTPLILKPTYLASSIGVTLITDt 175
Cdd:COG1181   75 LELLGIPytGSGVLASALAMDKALTKRVLAAAGLPTPPYVVLRrgELADLEAIEEELGLPLFVKPAREGSSVGVSKVKN- 153

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 389886429 176 etaEAEFNRVndylksinVPKAVTFEAPFIAEEFLQG 212
Cdd:COG1181  154 ---AEELAAA--------LEEAFKYDDKVLVEEFIDG 179
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 111-217 3.92e-07

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 49.55  E-value: 3.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429 111 QAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGTPLILKPTYLASSIGVTLITDtetaEAEFNRVNDYLK 190
Cdd:COG0189   89 EAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVED----EDALESILEALT 164

                         90       100
                 ....*....|....*....|....*...
gi 389886429 191 SinvpkavTFEAPFIAEEFLQGEYG-DW 217
Cdd:COG0189  165 E-------LGSEPVLVQEFIPEEDGrDI 185
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
 101-214 4.27e-07

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 49.72  E-value: 4.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429 101 ERLGLR--GAGVQAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGTPLILKPTYLASSIGVTLITDTEta 178
Cdd:PRK01372  79 ELLGIPytGSGVLASALAMDKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEED-- 156

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 389886429 179 eaefnrvndylksiNVPKAVTFEAPF----IAEEFLQG-EY 214
Cdd:PRK01372 157 --------------ELQAALELAFKYddevLVEKYIKGrEL 183
PurK COG0026
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ...
 81-210 1.36e-06

Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439797 [Multi-domain]  Cd Length: 353  Bit Score: 48.15  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  81 GVDAITTNNELFIAPMAKACERLGLRGAGVQAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGTPLILKP 160
Cdd:COG0026   52 RCDVVTFEFENVPAEALEALEAEVPVRPGPEALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKT 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 389886429 161 T------YlassiGVTLITDTETAEAEFNRVNdylksinvpkavtfEAPFIAEEFL 210
Cdd:COG0026  132 RrggydgK-----GQVVIKSAADLEAAWAALG--------------GGPCILEEFV 168
PRK07206 PRK07206
hypothetical protein; Provisional
 52-231 2.18e-06

hypothetical protein; Provisional


Pssm-ID: 180883 [Multi-domain]  Cd Length: 416  Bit Score: 47.72  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  52 PDSIYWAHEDHDKPEE----EVVEQIVKVAEMFGVDAITTNNELFIAPMAKACERLGLRGAGVQA-AENARDKNKMRDAF 126
Cdd:PRK07206  37 LDPYYYASFDTSDFIEviinGDIDDLVEFLRKLGPEAIIAGAESGVELADRLAEILTPQYSNDPAlSSARRNKAEMINAL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429 127 NKAGVKSIKNKRVTTLEDFRAALEE---IGTPLILKPTYLASSIGVTLITDTETAEAEFNRVndyLKSINVPKAVTFEAp 203
Cdd:PRK07206 117 AEAGLPAARQINTADWEEAEAWLREnglIDRPVVIKPLESAGSDGVFICPAKGDWKHAFNAI---LGKANKLGLVNETV- 192

                        170       180
                 ....*....|....*....|....*...
gi 389886429 204 fIAEEFLQGeygdwyqTEGYSDYISIEG 231
Cdd:PRK07206 193 -LVQEYLIG-------TEYVVNFVSLDG 212
carB PRK05294
carbamoyl-phosphate synthase large subunit;
107-162 2.28e-06

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 47.78  E-value: 2.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 389886429  107 GAGVQAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGTPLILKPTY 162
Cdd:PRK05294  117 GAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVIIRPSF 172
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 37-212 3.03e-06

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 47.69  E-value: 3.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429    37 IKDKDYFKSLAdFEHPDSIYwaheDHDKPEEEVVEqivkvaemFGvdAITTNNelfiapMAKACERLGLR--GAGVQAAE 114
Cdd:TIGR01369  607 TSDRLYFEPLT-FEDVMNII----ELEKPEGVIVQ--------FG--GQTPLN------LAKALEEAGVPilGTSPESID 665

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429   115 NARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGTPLILKPTYLASSIGVTLITDTETaeaefnrVNDYLKSINv 194
Cdd:TIGR01369  666 RAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEE-------LRRYLEEAV- 737

                          170
                   ....*....|....*...
gi 389886429   195 pkAVTFEAPFIAEEFLQG 212
Cdd:TIGR01369  738 --AVSPEHPVLIDKYLED 753
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 48-162 3.51e-06

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 47.18  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  48 DFEHPDSIYWahedhdkpEEEVVEQIVKVAEMFGVDAI-------TTNNelfiapMAKACERLGLR------GAGVQAAE 114
Cdd:COG0458   45 DYDTADRLYF--------EPLTVEDVLDIIEKEKPDGVivqfggqTALN------LAVELEEAGILegvkilGTSPDAID 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 389886429 115 NARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGTPLILKPTY 162
Cdd:COG0458  111 LAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
 54-215 8.52e-06

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 45.65  E-value: 8.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  54 SIYWAHEDHDKP---EEEVVEQIVKVAEMFGVDAITTNNELFIAPMAKACERLglRGAGVQA-------AENARDKNKMR 123
Cdd:PRK12767  39 ALYFADKFYVVPkvtDPNYIDRLLDICKKEKIDLLIPLIDPELPLLAQNRDRF--EEIGVKVlvsskevIEICNDKWLTY 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429 124 DAFNKAGVKSIKNKRVTTLEDFRAAL--EEIGTPLILKPTYLASSIGVTLITDTETAEAEFNRVNDYlksinvpkavtfe 201
Cdd:PRK12767 117 EFLKENGIPTPKSYLPESLEDFKAALakGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPNL------------- 183

                        170
                 ....*....|....*
gi 389886429 202 apfIAEEFLQG-EYG 215
Cdd:PRK12767 184 ---IIQEFIEGqEYT 195
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 70-159 2.29e-05

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 45.07  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429   70 VEQIVKVAEMFGVDAI-------TTNNELfiapmAKACERLGLR--GAGVQAAENARDKNKMRDAFNKAGVKSIK--NKR 138
Cdd:COG1038    66 IEEIIRVAKEKGVDAIhpgygflSENPEF-----ARACEEAGITfiGPSPEVLEMLGDKVAARAAAIEAGVPVIPgtEGP 140

                          90       100
                  ....*....|....*....|.
gi 389886429  139 VTTLEDFRAALEEIGTPLILK 159
Cdd:COG1038   141 VDDLEEALAFAEEIGYPVMLK 161
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
59-225 3.72e-05

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 43.76  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  59 HEDHDKPEEEVVEQIVKVAEMFGVDAITTNNELFIAPMAKACERLGLR----GAGVQAAENARDKNKMRDAFNKAGVKSI 134
Cdd:COG3919   54 VPDPGDDPEAFVDALLELAERHGPDVLIPTGDEYVELLSRHRDELEEHyrlpYPDADLLDRLLDKERFYELAEELGVPVP 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429 135 KNKRVTTLEDFRAALEEIGTPLILKPTY--LASSIGVTLITDTETAE--AEFNRVndylksinVPKAVTFEAPFIAEEFL 210
Cdd:COG3919  134 KTVVLDSADDLDALAEDLGFPVVVKPADsvGYDELSFPGKKKVFYVDdrEELLAL--------LRRIAAAGYELIVQEYI 205

                        170
                 ....*....|....*
gi 389886429 211 QGEYGDWYQTEGYSD 225
Cdd:COG3919  206 PGDDGEMRGLTAYVD 220
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 70-159 4.64e-05

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 43.97  E-value: 4.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429   70 VEQIVKVAEMFGVDAI-------TTNNELfiapmAKACERLGLR--GAGVQAAENARDKNKMRDAFNKAGVKSIK--NKR 138
Cdd:PRK12999   67 IDEIIRVAKQAGVDAIhpgygflSENPEF-----ARACAEAGITfiGPTAEVLRLLGDKVAARNAAIKAGVPVIPgsEGP 141

                          90       100
                  ....*....|....*....|.
gi 389886429  139 VTTLEDFRAALEEIGTPLILK 159
Cdd:PRK12999  142 IDDIEEALEFAEEIGYPIMLK 162
ATP-grasp_4 pfam13535
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 152-213 5.41e-05

ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 316093 [Multi-domain]  Cd Length: 160  Bit Score: 42.27  E-value: 5.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 389886429  152 IGTPLILKPTYLASSIGVTLITDTETAEAEFNRVNDYLKSINV--PKAVTFEAPFIAEEFLQGE 213
Cdd:pfam13535   1 IPYPCVIKPSVGFFSVGVYKINNREEWKAAFAAIREEIEQWKEmyPEAVVDGGSFLVEEYIEGE 64
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
 107-162 8.30e-05

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 43.06  E-value: 8.30e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 389886429   107 GAGVQAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGTPLILKPTY 162
Cdd:TIGR01369  116 GTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPVIVRPAF 171
PRK06019 PRK06019
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
 70-159 1.59e-04

phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed


Pssm-ID: 235674 [Multi-domain]  Cd Length: 372  Bit Score: 42.06  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  70 VEQIVKVAEmfGVDAITTNNElFI--APMAKACERLGLRgAGVQAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRA 147
Cdd:PRK06019  54 VAALRELAE--QCDVITYEFE-NVpaEALDALAARVPVP-PGPDALAIAQDRLTEKQFLDKLGIPVAPFAVVDSAEDLEA 129

                         90
                 ....*....|..
gi 389886429 148 ALEEIGTPLILK 159
Cdd:PRK06019 130 ALADLGLPAVLK 141
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
 70-182 6.11e-04

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 40.40  E-value: 6.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  70 VEQIVKVAEMFGVDAI------TTNNELFiapmAKACERLGLRGAGVQAAENAR--DKNKMRDAFNKAGVKSIKNKRvTT 141
Cdd:PRK06111  63 LEKIIEIAKKTGAEAIhpgyglLSENASF----AERCKEEGIVFIGPSADIIAKmgSKIEARRAMQAAGVPVVPGIT-TN 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 389886429 142 LEDFRAALE---EIGTPLILKPTYLASSIGVTLITDTETAEAEF 182
Cdd:PRK06111 138 LEDAEEAIAiarQIGYPVMLKASAGGGGIGMQLVETEQELTKAF 181
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
 70-182 7.87e-04

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 40.12  E-value: 7.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  70 VEQIVKVAEMFGVDAI------TTNNELFiapmAKACERLGLRGAGVQAAENAR--DKNKMRDAFNKAGVKSI--KNKRV 139
Cdd:PRK12833  66 PAAILAAARQCGADAIhpgygfLSENAAF----AEAVEAAGLIFVGPDAQTIRTmgDKARARRTARRAGVPTVpgSDGVV 141

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 389886429 140 TTLEDFRAALEEIGTPLILKPTYLASSIGVTLITDTETAEAEF 182
Cdd:PRK12833 142 ASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAEL 184
PLN02257 PLN02257
phosphoribosylamine--glycine ligase
 107-213 8.27e-04

phosphoribosylamine--glycine ligase


Pssm-ID: 177899 [Multi-domain]  Cd Length: 434  Bit Score: 40.11  E-value: 8.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429 107 GAGVQAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGTPLILKPTYLASSIGVTLITDTETAeaeFNRVN 186
Cdd:PLN02257  91 GPSAEAAALEGSKNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKGVVVAMTLEEA---YEAVD 167

                         90       100
                 ....*....|....*....|....*..
gi 389886429 187 DYLKSINVPKAvtfEAPFIAEEFLQGE 213
Cdd:PLN02257 168 SMLVKGAFGSA---GSEVVVEEFLDGE 191
PurD COG0151
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ...
 122-213 9.80e-04

Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439921 [Multi-domain]  Cd Length: 422  Bit Score: 39.61  E-value: 9.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429 122 MRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGTPLILKPTYLASSIGVTLITDTETAEAefnrvndYLKSINVPKAvtFE 201
Cdd:COG0151  106 AKEFMARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKGVVVAETLEEALA-------AVDDMLADGK--FG 176

                         90
                 ....*....|....*
gi 389886429 202 ---APFIAEEFLQGE 213
Cdd:COG0151  177 dagARVVIEEFLEGE 191
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
70-192 1.09e-03

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 39.58  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  70 VEQIVKVAEMFGVDAI-------TTNNELfiapmAKACERLGLR--GAGVQAAENARDKNKMRDAFNKAGVKSI--KNKR 138
Cdd:PRK08654  63 IERIIDVAKKAGADAIhpgygflAENPEF-----AKACEKAGIVfiGPSSDVIEAMGSKINAKKLMKKAGVPVLpgTEEG 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 389886429 139 VTTLEDFRAALEEIGTPLILKPTYLASSIGVTLITDtetaEAEFNRVNDYLKSI 192
Cdd:PRK08654 138 IEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYS----EEELEDAIESTQSI 187
ddl PRK01966
D-alanine--D-alanine ligase;
107-182 2.22e-03

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 38.56  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429 107 GAGVQAAENARDKNKMRDAFNKAGVKSIK----NKRVTTLEDFRAALEEIGTPLILKPTYLASSIGVTLITDtetaEAEF 182
Cdd:PRK01966 112 GCGVLASALSMDKILTKRLLAAAGIPVAPyvvlTRGDWEEASLAEIEAKLGLPVFVKPANLGSSVGISKVKN----EEEL 187
PLN02735 PLN02735
carbamoyl-phosphate synthase
 105-162 3.49e-03

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 38.22  E-value: 3.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 389886429  105 LRGAGVQAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGT-PLILKPTY 162
Cdd:PLN02735  131 LIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGEfPLIIRPAF 189
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 111-199 4.36e-03

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 37.33  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  111 QAAENARDKNKMRDAFNKAGVKSIKNKRVTTLEDFRAALEEIGTPLILKPTYLASSIGVTLITDTETAEA---EFNRVND 187
Cdd:TIGR00768  81 DAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESlleHFEQLNG 160

                          90
                  ....*....|..
gi 389886429  188 YLKSINVPKAVT 199
Cdd:TIGR00768 161 PQNLFLVQEYIK 172
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
 47-174 6.52e-03

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 37.26  E-value: 6.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429   47 ADFEHPDSIYWahedhdkpEEEVVEQIVKVAEMFGVDAI-------TTNNelfiapMAKACERLGLRGAGVQAaeNARDK 119
Cdd:PRK12815  604 TDYDTADRLYF--------EPLTLEDVLNVAEAENIKGVivqfggqTAIN------LAKGLEEAGLTILGTSP--DTIDR 667

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 389886429  120 NKMRDAF----NKAGVKSIKNKRVTTLEDFRAALEEIGTPLILKPTYLASSIGVTLITD 174
Cdd:PRK12815  668 LEDRDRFyqllDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYD 726
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
73-182 9.64e-03

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 36.65  E-value: 9.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389886429  73 IVKVAEMFGVDAI------TTNNELFIapmaKACERLGLR--GAGVQAAENARDKNKMRDAFNKAGVKSIKNKR--VTTL 142
Cdd:PRK08462  68 IISAAEIFEADAIfpgygfLSENQNFV----EICSHHNIKfiGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDgaLKSY 143

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 389886429 143 EDFRAALEEIGTPLILKPTYLASSIGVTLITDTETAEAEF 182
Cdd:PRK08462 144 EEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLY 183
 
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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