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Conserved domains on  [gi|1176771985|gb|OQY89861|]
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MAG: hypothetical protein B6D38_05555 [Anaerolineae bacterium UTCFX1]

Protein Classification

MaoC family dehydratase( domain architecture ID 10130975)

MaoC family dehydratase similar to Aeromonas caviae (R)-specific enoyl-CoA hydratase that is involved in polyhydroxyalkanoate biosynthesis, and Methylorubrum extorquens 3-hydroxybutyryl-CoA dehydratase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 8-132 4.14e-54

(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.


:

Pssm-ID: 239533 [Multi-domain]  Cd Length: 128  Bit Score: 165.80  E-value: 4.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985   8 KEGDGFSFERFISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAFLGGLISKALGVDFPGEGAVYILQNSAFKR 87
Cdd:cd03449     2 KVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFLR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1176771985  88 PVFVDSIVRVEIKVTQVNSEKRRLALDTTILNADGKACLVGSAEV 132
Cdd:cd03449    82 PVFIGDTVTATVTVTEKREDKKRVTLETVCTNQNGEVVIEGEAVV 126
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 8-132 4.14e-54

(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.


Pssm-ID: 239533 [Multi-domain]  Cd Length: 128  Bit Score: 165.80  E-value: 4.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985   8 KEGDGFSFERFISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAFLGGLISKALGVDFPGEGAVYILQNSAFKR 87
Cdd:cd03449     2 KVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFLR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1176771985  88 PVFVDSIVRVEIKVTQVNSEKRRLALDTTILNADGKACLVGSAEV 132
Cdd:cd03449    82 PVFIGDTVTATVTVTEKREDKKRVTLETVCTNQNGEVVIEGEAVV 126
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
7-135 7.95e-34

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 114.98  E-value: 7.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985   7 FKEGDGFSFERF-ISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAFLGGLISKALGVDFPGEG-AVYILQNSA 84
Cdd:COG2030     5 LEVGDVLPHGGRtVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAvANLGLQEVR 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1176771985  85 FKRPVFVDSIVRVEIKVTQVNSEKRR--LALDTTILNADGKACLVGSAEVWLP 135
Cdd:COG2030    85 FLRPVRVGDTLRARVEVLEKRESKSRgiVTLRTTVTNQDGEVVLTGEATVLVP 137
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 10-135 2.78e-32

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 118.06  E-value: 2.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985  10 GDGFSFERFISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAFLGGLISKALGVDFPGEGAVYILQNSAFKRPV 89
Cdd:PRK08190   17 GDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGTRLPGPGTIYLGQSLRFRRPV 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1176771985  90 FVDSIVRVEIKVTQVNSEKRRLALDTTILNADGKACLVGSAEVWLP 135
Cdd:PRK08190   97 RIGDTLTVTVTVREKDPEKRIVVLDCRCTNQDGEVVITGTAEVIAP 142
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 12-102 4.69e-13

MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.


Pssm-ID: 396243 [Multi-domain]  Cd Length: 123  Bit Score: 61.20  E-value: 4.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985  12 GFSFERFISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAFLGGLISKALGVDFPGEG-AVYILQNSAFKRPVF 90
Cdd:pfam01575  11 DTEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNViARFGEIKVRFTKPVF 90

                          90
                  ....*....|..
gi 1176771985  91 VDSIVRVEIKVT 102
Cdd:pfam01575  91 PGDTLRTEAEVV 102
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 8-132 4.14e-54

(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.


Pssm-ID: 239533 [Multi-domain]  Cd Length: 128  Bit Score: 165.80  E-value: 4.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985   8 KEGDGFSFERFISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAFLGGLISKALGVDFPGEGAVYILQNSAFKR 87
Cdd:cd03449     2 KVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFLR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1176771985  88 PVFVDSIVRVEIKVTQVNSEKRRLALDTTILNADGKACLVGSAEV 132
Cdd:cd03449    82 PVFIGDTVTATVTVTEKREDKKRVTLETVCTNQNGEVVIEGEAVV 126
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
7-135 7.95e-34

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 114.98  E-value: 7.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985   7 FKEGDGFSFERF-ISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAFLGGLISKALGVDFPGEG-AVYILQNSA 84
Cdd:COG2030     5 LEVGDVLPHGGRtVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAvANLGLQEVR 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1176771985  85 FKRPVFVDSIVRVEIKVTQVNSEKRR--LALDTTILNADGKACLVGSAEVWLP 135
Cdd:COG2030    85 FLRPVRVGDTLRARVEVLEKRESKSRgiVTLRTTVTNQDGEVVLTGEATVLVP 137
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 10-135 2.78e-32

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 118.06  E-value: 2.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985  10 GDGFSFERFISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAFLGGLISKALGVDFPGEGAVYILQNSAFKRPV 89
Cdd:PRK08190   17 GDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGTRLPGPGTIYLGQSLRFRRPV 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1176771985  90 FVDSIVRVEIKVTQVNSEKRRLALDTTILNADGKACLVGSAEVWLP 135
Cdd:PRK08190   97 RIGDTLTVTVTVREKDPEKRIVVLDCRCTNQDGEVVITGTAEVIAP 142
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 10-132 4.17e-30

(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. The structure of the monomer includes a five-strand antiparallel beta-sheet wrapped around a central alpha helix, referred to as a hot dog fold. The active site lies within a substrate-binding tunnel formed by the homodimer. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit.


Pssm-ID: 239525 [Multi-domain]  Cd Length: 127  Bit Score: 105.04  E-value: 4.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985  10 GDGFSFERFISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAFLGGLISKALGVDFPGE-GAVYILQNSAFKRP 88
Cdd:cd03441     1 GELDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTdGANLGSQSVRFLAP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1176771985  89 VFVDSIVRVEIKVTQV--NSEKRRLALDTTILNADGKACLVGSAEV 132
Cdd:cd03441    81 VFPGDTLRVEVEVLGKrpSKGRGVVTVRTEARNQGGEVVLSGEATV 126
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 7-122 3.86e-13

MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but without the N-terminal PutA domain. This protein family has a hot-dog fold similar to that of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239530 [Multi-domain]  Cd Length: 140  Bit Score: 61.94  E-value: 3.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985   7 FKEGDGF-SFERFISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAF----LGGLISKALGVDFPGEgAVYILQ 81
Cdd:cd03446     5 FEIGQVFeSVGRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLtlsiATGLLQRLGVFERTVV-AFYGID 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1176771985  82 NSAFKRPVFV-DSI-VRVEIKVTQVNSEKR--RLALDTTILNADG 122
Cdd:cd03446    84 NLRFLNPVFIgDTIrAEAEVVEKEEKDGEDagVVTRRIEVVNQRG 128
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 12-102 4.69e-13

MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.


Pssm-ID: 396243 [Multi-domain]  Cd Length: 123  Bit Score: 61.20  E-value: 4.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985  12 GFSFERFISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAFLGGLISKALGVDFPGEG-AVYILQNSAFKRPVF 90
Cdd:pfam01575  11 DTEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNViARFGEIKVRFTKPVF 90

                          90
                  ....*....|..
gi 1176771985  91 VDSIVRVEIKVT 102
Cdd:pfam01575  91 PGDTLRTEAEVV 102
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 17-103 1.12e-11

MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory protein. Orthologs of MaoC include PaaZ [Escherichia coli] and PaaN [Pseudomonas putida], which are putative ring-opening enzymes involved in phenylacetic acid degradation. The C-terminal domain of MaoC has sequence similarity to (R)-specific enoyl-CoA hydratase,Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. MaoC also has an N-terminal PutA domain like that found in the E. coli PutA proline dehydrogenase and other members of the aldehyde dehydrogenase family.


Pssm-ID: 239536 [Multi-domain]  Cd Length: 142  Bit Score: 58.18  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985  17 RFISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAFlggLISKALG--VDfPGEGAV---YILQNSAFKRPVFV 91
Cdd:cd03452    16 RTVTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHGYF---VLSAAAGlfVD-PAPGPVlanYGLENLRFLEPVYP 91

                          90
                  ....*....|..
gi 1176771985  92 DSIVRVEIKVTQ 103
Cdd:cd03452    92 GDTIQVRLTCKR 103
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 19-132 6.03e-09

SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot dog fold that is similar to those of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239537 [Multi-domain]  Cd Length: 127  Bit Score: 50.78  E-value: 6.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985  19 ISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHG----AFLGGLISKALGvdfpGEGAVYILQNSaFKRPVFV-DS 93
Cdd:cd03453    12 VSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGmltmGLLGRLVTDWVG----DPGRVVSFGVR-FTKPVPVpDT 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1176771985  94 IV-RVEIKVTQVNSEKRRLALDTTILNADGKACLVGSAEV 132
Cdd:cd03453    87 LTcTGIVVEKTVADGEDALTVTVDATDQAGGKKVLGRAIV 126
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 12-123 4.05e-07

N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of MaoC dehydratase, pfam01575, that the full-length functional dehydratase enzyme is made up of two structures that dimerize to form a whole. Divergence of the N- and C- monomers in higher eukaryotes has led to two distinct domains, this one and MaoC_dehydratas. However, in order to function as an enzyme both are required together.


Pssm-ID: 433220 [Multi-domain]  Cd Length: 132  Bit Score: 45.76  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985  12 GFSFERF---ISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAFLGGLISKALG----VDFPGEGAVYILQNSA 84
Cdd:pfam13452   4 GVEFGPVkyeVERGAIREFARAIGETNPAYWDEAAARAAGYGDLPAPPTFLFVLGWDAPGfmeqLGIDLSRLLHGEQRFT 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1176771985  85 FKRPVFVDSIVRVEIKVTQVNSEKRRLALD-----TTILNADGK 123
Cdd:pfam13452  84 YHRPLRAGDELTCRSQIADVYDKKGNGALCfvvveTEVTNQRGE 127
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 52-132 7.83e-07

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 44.39  E-value: 7.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985  52 RIVHGAFLGGLISKALG-----VDFPGEGAVYILQNSAFKRPVFVDSIVRVEIKVTQVnsEKRRLALDTTILNADGKACL 126
Cdd:cd03440    16 GIVHGGLLLALADEAAGaaaarLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRV--GRSSVTVEVEVRNEDGKLVA 93


                  ....*.
gi 1176771985 127 VGSAEV 132
Cdd:cd03440    94 TATATF 99
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 7-135 3.41e-06

YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown function. YdeM has sequence similarity to the hot-dog fold of (R)-specific enoyl-CoA hydratase. Other enzymes with this fold include the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239538 [Multi-domain]  Cd Length: 140  Bit Score: 43.71  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985   7 FKEGDGFSF-ERFISADDVKKFAEiVGDSNPIHLDESFAERSFFkkrivhgaflGGLI---------SKALGVD-FPGEG 75
Cdd:cd03454     4 LVIGQRFTSgSYTVTEEEIIAFAR-EFDPQPFHLDEEAAKESLF----------GGLAasgwhtaaiTMRLLVDaGLSGS 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1176771985  76 AVYI---LQNSAFKRPVFVDSIVRVEIKVTQVNSEKRR-----LALDTTILNADGKACLVGSAEVWLP 135
Cdd:cd03454    73 ASGGspgIDELRWPRPVRPGDTLSVEVEVLDKRPSRSRpdrgiVTLRSETLNQRGEVVLTFEATVLVR 140
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 7-102 1.49e-05

FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved family of proteins found in prokaryotes and archaea but not in eukaryotes. FkbR2 has sequence similarity to (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The function of FkbR2 is unknown.


Pssm-ID: 239535 [Multi-domain]  Cd Length: 146  Bit Score: 41.81  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985   7 FKEGDGF--SFERFISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAFlggLISKALGVDFPG--EGAVYIL-- 80
Cdd:cd03451     7 FTVGQVFehAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLF---TLSLALGLSVNDtsLTAVANLgy 83

                          90       100
                  ....*....|....*....|..
gi 1176771985  81 QNSAFKRPVFVDSIVRVEIKVT 102
Cdd:cd03451    84 DEVRFPAPVFHGDTLYAESEVL 105
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 32-67 2.90e-04

HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), and Hydratase-Dehydrogenase-Epimerase (HDE) proteins. Other enzymes with this fold include MaoC dehydratase, and the fatty acid synthase beta subunit.


Pssm-ID: 239532 [Multi-domain]  Cd Length: 122  Bit Score: 37.97  E-value: 2.90e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1176771985  32 GDSNPIHLDESFAERSFFKKRIVHGAFLGGLISKAL 67
Cdd:cd03448    25 GDYNPLHIDPAFAKAAGFPRPILHGLCTYGFAARAV 60
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 27-132 4.03e-04

FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and 17-beta-hydroxysteriod dehydrogenase (HSD).


Pssm-ID: 239531 [Multi-domain]  Cd Length: 126  Bit Score: 37.64  E-value: 4.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985  27 FAEIVGDSNPIHLDESFAERSFFKKRIVHGAFLGGLISKALGVDFpGEGAVYILQ--NSAFKRPVFVDSIVRVEIKVTQV 104
Cdd:cd03447    18 YARVSGDFNPIHVSRVFASYAGLPGTITHGMYTSAAVRALVETWA-ADNDRSRVRsfTASFVGMVLPNDELEVRLEHVGM 96

                          90       100
                  ....*....|....*....|....*...
gi 1176771985 105 NSEKRRLALDTTIlNADGKACLVGSAEV 132
Cdd:cd03447    97 VDGRKVIKVEARN-EETGELVLRGEAEV 123
NodN cd03450
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal ...
 19-117 5.80e-03

NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. Rhizobium and related species form nodules on the roots of their legume hosts, a symbiotic process that requires production of Nod factors, which are signal molecules involved in root hair deformation and meristematic cell division. The nodulation gene products, including NodN, are involved in producing the Nod factors, however the role played by NodN is unclear.


Pssm-ID: 239534 [Multi-domain]  Cd Length: 149  Bit Score: 34.85  E-value: 5.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176771985  19 ISADDVKKFAEIVGDSNPIHLDESFAERSFFKKRIVHGAFLGGLISKALGVDFPGEGAV----YILQNSAFKRPVFVDSI 94
Cdd:cd03450    24 VDQERIDQFADATGDHQWIHVDPERAAAEPFGGTIAHGFLTLSLLPALTPQLFRVEGVKmgvnYGLDKVRFPAPVPVGSR 103

                          90       100
                  ....*....|....*....|....*.
gi 1176771985  95 VRVEIKVTQVNSEKR---RLALDTTI 117
Cdd:cd03450   104 VRGRFTLLSVEELKGggvQVTLEVTV 129
 
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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