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Conserved domains on  [gi|2158796580|dbj|GJC69794|]
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hypothetical protein KAM406_02740 [Acinetobacter sp. KAM406]

Protein Classification

Rossmann-like and DUF2520 domain-containing protein( domain architecture ID 11475612)

Rossmann-like and DUF2520 domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-258 7.60e-86

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


:

Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 257.05  E-value: 7.60e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   1 MRIGLIGAGRVAHHLAHVL-NAQHQIVQIYSRSLDKAQDLAAQVGAEAIAEVEQLHSDLDLLIIAVSDQAIAQVIQEIH- 78
Cdd:COG5495     4 MKIGIIGAGRVGTALAAALrAAGHEVVGVYSRSPASAERAAALLGAVPALDLEELAAEADLVLLAVPDDAIAEVAAGLAa 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580  79 --HDLNHVLIVHTSGSTKLDVLQQHH---ARSGVFYPLQTFSLEREI--DWTETPLFIEAAfAEDQQLLMTLANSLSKKV 151
Cdd:COG5495    84 agALRPGQLVVHTSGALGSDVLAPAAragALTGSFHPLQTFSGPREDleRLAGIPFAIEGD-EEALPVLEALAEALGGEP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580 152 YAYTSEQRLSLHLAAVFACNFSNYCYDMAKQVVDDQQVD--FSLLYPLMMETAHKATQNDPRKMQTGPAMRGDRNILNMH 229
Cdd:COG5495   163 FVIDSEQRPLYHAAAVFASNFLVTLVALAAELLEAAGLEdaFDALLPLIRETLDNILELGPAAALTGPAARGDAGTVAKH 242

                         250       260
                  ....*....|....*....|....*....
gi 2158796580 230 QDVLAAGQQyALAEVYTLMSQQILERHQS 258
Cdd:COG5495   243 LAALAELDP-ELAELYRALSRSTLELAGK 270
 
Name Accession Description Interval E-value
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-258 7.60e-86

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 257.05  E-value: 7.60e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   1 MRIGLIGAGRVAHHLAHVL-NAQHQIVQIYSRSLDKAQDLAAQVGAEAIAEVEQLHSDLDLLIIAVSDQAIAQVIQEIH- 78
Cdd:COG5495     4 MKIGIIGAGRVGTALAAALrAAGHEVVGVYSRSPASAERAAALLGAVPALDLEELAAEADLVLLAVPDDAIAEVAAGLAa 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580  79 --HDLNHVLIVHTSGSTKLDVLQQHH---ARSGVFYPLQTFSLEREI--DWTETPLFIEAAfAEDQQLLMTLANSLSKKV 151
Cdd:COG5495    84 agALRPGQLVVHTSGALGSDVLAPAAragALTGSFHPLQTFSGPREDleRLAGIPFAIEGD-EEALPVLEALAEALGGEP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580 152 YAYTSEQRLSLHLAAVFACNFSNYCYDMAKQVVDDQQVD--FSLLYPLMMETAHKATQNDPRKMQTGPAMRGDRNILNMH 229
Cdd:COG5495   163 FVIDSEQRPLYHAAAVFASNFLVTLVALAAELLEAAGLEdaFDALLPLIRETLDNILELGPAAALTGPAARGDAGTVAKH 242

                         250       260
                  ....*....|....*....|....*....
gi 2158796580 230 QDVLAAGQQyALAEVYTLMSQQILERHQS 258
Cdd:COG5495   243 LAALAELDP-ELAELYRALSRSTLELAGK 270
DUF2520 pfam10728
Domain of unknown function (DUF2520); This presumed domain is found C-terminal to a ...
 125-251 1.97e-37

Domain of unknown function (DUF2520); This presumed domain is found C-terminal to a Rossmann-like domain suggesting that these proteins are oxidoreductases.


Pssm-ID: 463182  Cd Length: 126  Bit Score: 127.95  E-value: 1.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580 125 TPLFIEAAfAEDQQLLMTLANSLSKKVYAYTSEQRLSLHLAAVFACNFSNYCYDMAKQVVDDQQVD--FSLLYPLMMETA 202
Cdd:pfam10728   1 IPFGIEGD-EEALAVLEALAESLGGKVFEIDSEQRKLYHAAAVFASNFLVTLYALAAELLEEAGLPeaFEALLPLIRETL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2158796580 203 HKATQNDPRKMQTGPAMRGDRNILNMHQDVLAAGQQyaLAEVYTLMSQQ 251
Cdd:pfam10728  80 DNILELGPVAALTGPVARGDAGTVAKHLAALADDPE--LAELYRLLSRS 126
PRK13304 PRK13304
aspartate dehydrogenase;
1-87 6.41e-08

aspartate dehydrogenase;


Pssm-ID: 237343 [Multi-domain]  Cd Length: 265  Bit Score: 52.30  E-value: 6.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   1 MRIGLIGAGRVAHHLAHVLNAQH---QIVQIYSRSLDKAQDLAAQVGAEAIAEVEQLHSDLDLLIIAVSDQAIAQVIQEI 77
Cdd:PRK13304    2 LKIGIVGCGAIASLITKAILSGRinaELYAFYDRNLEKAENLASKTGAKACLSIDELVEDVDLVVECASVNAVEEVVPKS 81

                          90
                  ....*....|
gi 2158796580  78 HHDLNHVLIV 87
Cdd:PRK13304   82 LENGKDVIIM 91
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 2-77 2.72e-04

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 41.48  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   2 RIGLIGAGR----VAHHLAhvlNAQHQIVQIYSRSLDKAQDLAAQVGAEAI--AEVEQLHSDLDLLIIAVSDQAIAQVIQ 75
Cdd:cd05213   180 KVLVIGAGEmgelAAKHLA---AKGVAEITIANRTYERAEELAKELGGNAVplDELLELLNEADVVISATGAPHYAKIVE 256


                  ..
gi 2158796580  76 EI 77
Cdd:cd05213   257 RA 258
TraI_TIGR TIGR02760
conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome ...
 15-138 5.34e-03

conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome complex. In the process of conjugative plasmid transfer the realaxosome binds to the plasmid at the oriT (origin of transfer) site. The relaxase protein TraI mediates the single-strand nicking and ATP-dependent unwinding (relaxation, helicase activity) of the plasmid molecule. These two activities reside in separate domains of the protein.


Pssm-ID: 274285 [Multi-domain]  Cd Length: 1960  Bit Score: 37.96  E-value: 5.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   15 LAHVLNAQHQIVQIYSRSLDKAQDLA--AQVGAEAIAEVEQLHSDLDLLIIAVSDQAiaqviqeIHHDLNHVLIVHTSGS 92
Cdd:TIGR02760  833 LLNSLNRSASRVDLFTDLDEKAQRYLekTRGIPSAIVVVDQKQHLPDAVTTNNTDKS-------LEMDISDTLHALEAKA 905

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2158796580   93 tkldvlQQHHARSGVFYPLQTFSlEREIDWTETPLFIEA-AFAEDQQ 138
Cdd:TIGR02760  906 ------KDGKNSIALQYALEKVS-EKEAAFKQKELVTEAyVFAFEET 945
 
Name Accession Description Interval E-value
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-258 7.60e-86

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 257.05  E-value: 7.60e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   1 MRIGLIGAGRVAHHLAHVL-NAQHQIVQIYSRSLDKAQDLAAQVGAEAIAEVEQLHSDLDLLIIAVSDQAIAQVIQEIH- 78
Cdd:COG5495     4 MKIGIIGAGRVGTALAAALrAAGHEVVGVYSRSPASAERAAALLGAVPALDLEELAAEADLVLLAVPDDAIAEVAAGLAa 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580  79 --HDLNHVLIVHTSGSTKLDVLQQHH---ARSGVFYPLQTFSLEREI--DWTETPLFIEAAfAEDQQLLMTLANSLSKKV 151
Cdd:COG5495    84 agALRPGQLVVHTSGALGSDVLAPAAragALTGSFHPLQTFSGPREDleRLAGIPFAIEGD-EEALPVLEALAEALGGEP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580 152 YAYTSEQRLSLHLAAVFACNFSNYCYDMAKQVVDDQQVD--FSLLYPLMMETAHKATQNDPRKMQTGPAMRGDRNILNMH 229
Cdd:COG5495   163 FVIDSEQRPLYHAAAVFASNFLVTLVALAAELLEAAGLEdaFDALLPLIRETLDNILELGPAAALTGPAARGDAGTVAKH 242

                         250       260
                  ....*....|....*....|....*....
gi 2158796580 230 QDVLAAGQQyALAEVYTLMSQQILERHQS 258
Cdd:COG5495   243 LAALAELDP-ELAELYRALSRSTLELAGK 270
DUF2520 pfam10728
Domain of unknown function (DUF2520); This presumed domain is found C-terminal to a ...
 125-251 1.97e-37

Domain of unknown function (DUF2520); This presumed domain is found C-terminal to a Rossmann-like domain suggesting that these proteins are oxidoreductases.


Pssm-ID: 463182  Cd Length: 126  Bit Score: 127.95  E-value: 1.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580 125 TPLFIEAAfAEDQQLLMTLANSLSKKVYAYTSEQRLSLHLAAVFACNFSNYCYDMAKQVVDDQQVD--FSLLYPLMMETA 202
Cdd:pfam10728   1 IPFGIEGD-EEALAVLEALAESLGGKVFEIDSEQRKLYHAAAVFASNFLVTLYALAAELLEEAGLPeaFEALLPLIRETL 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2158796580 203 HKATQNDPRKMQTGPAMRGDRNILNMHQDVLAAGQQyaLAEVYTLMSQQ 251
Cdd:pfam10728  80 DNILELGPVAALTGPVARGDAGTVAKHLAALADDPE--LAELYRLLSRS 126
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
4-87 4.60e-10

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 54.93  E-value: 4.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   4 GLIGAGRVAHHLAHVLNAQ--HQIVQIYSRSLDKAQDLAAQVGAEAIA-EVEQLHSDLDLLIIAVSDQAIAQVIQEIHHD 80
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAgpHEVVVANSRNPEKAEELAEEYGVGATAvDNEEAAEEADVVFLAVKPEDAPDVLSELSDL 80


                  ....*..
gi 2158796580  81 LNHVLIV 87
Cdd:pfam03807  81 LKGKIVI 87
AspD COG1712
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];
1-73 4.95e-09

L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];


Pssm-ID: 441318 [Multi-domain]  Cd Length: 263  Bit Score: 55.58  E-value: 4.95e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2158796580   1 MRIGLIGAGRVAHHLA-HVLNAQHQIVQIYSRSLDKAQDLAAQVGAEAIAEVEQL-HSDLDLLIIAVSDQAIAQV 73
Cdd:COG1712     1 MRIGLIGCGAIGSEVAeALADAGVELVAVYDRDPERAEALLASLGARVVSDVDELlAADPDLVVEAASQAAVREH 75
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-86 5.13e-08

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 52.37  E-value: 5.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   1 MRIGLIGAGRVAHHLAHVLNAQ----HQIVqIYSRSLDKAQDLAAQVGAEAIAEVEQLHSDLDLLIIAVSDQAIAQVIQE 76
Cdd:COG0345     3 MKIGFIGAGNMGSAIIKGLLKSgvppEDII-VSDRSPERLEALAERYGVRVTTDNAEAAAQADVVVLAVKPQDLAEVLEE 81

                          90
                  ....*....|..
gi 2158796580  77 IHHDL--NHVLI 86
Cdd:COG0345    82 LAPLLdpDKLVI 93
PRK13304 PRK13304
aspartate dehydrogenase;
1-87 6.41e-08

aspartate dehydrogenase;


Pssm-ID: 237343 [Multi-domain]  Cd Length: 265  Bit Score: 52.30  E-value: 6.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   1 MRIGLIGAGRVAHHLAHVLNAQH---QIVQIYSRSLDKAQDLAAQVGAEAIAEVEQLHSDLDLLIIAVSDQAIAQVIQEI 77
Cdd:PRK13304    2 LKIGIVGCGAIASLITKAILSGRinaELYAFYDRNLEKAENLASKTGAKACLSIDELVEDVDLVVECASVNAVEEVVPKS 81

                          90
                  ....*....|
gi 2158796580  78 HHDLNHVLIV 87
Cdd:PRK13304   82 LENGKDVIIM 91
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-69 4.29e-07

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 49.92  E-value: 4.29e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2158796580   1 MRIGLIGAGRVAHHLAHVL--NAQHQIVQIYSRSLDKAQDLAAQVGAEAIAEVEQL--HSDLDLLIIAVSDQA 69
Cdd:COG0673     4 LRVGIIGAGGIGRAHAPALaaLPGVELVAVADRDPERAEAFAEEYGVRVYTDYEELlaDPDIDAVVIATPNHL 76
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-92 2.29e-06

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 47.80  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   1 MRIGLIGAGRVAHHLA-HVLNAQHQiVQIYSRSLDKAQDLAAQvGAEAIAEVEQLHSDLDLLIIAVSD-QAIAQVIQEIH 78
Cdd:COG2084     2 MKVGFIGLGAMGAPMArNLLKAGHE-VTVWNRTPAKAEALVAA-GARVAASPAEAAAAADVVITMLPDdAAVEEVLLGED 79

                          90
                  ....*....|....*....
gi 2158796580  79 HDLNH-----VLIVHTSGS 92
Cdd:COG2084    80 GLLAAlrpgaVVVDMSTIS 98
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-86 2.77e-06

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 47.45  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   1 MRIGLIGAGRVAHHLAHVLNAQ----HQIVqIYSRSLDKAQDLAAQVGAEAIAEVEQLHSDLDLLIIAVSDQAIAQVIQE 76
Cdd:PRK11880    3 KKIGFIGGGNMASAIIGGLLASgvpaKDII-VSDPSPEKRAALAEEYGVRAATDNQEAAQEADVVVLAVKPQVMEEVLSE 81

                          90
                  ....*....|
gi 2158796580  77 IHHDLNHVLI 86
Cdd:PRK11880   82 LKGQLDKLVV 91
GFO_IDH_MocA pfam01408
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ...
 1-77 3.77e-06

Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.


Pssm-ID: 426248 [Multi-domain]  Cd Length: 120  Bit Score: 44.89  E-value: 3.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   1 MRIGLIGAGRVAHHLAHVLNA---QHQIVQIYSRSLDKAQDLAAQVGAEAIAEVEQL--HSDLDLLIIAVSDQAIAQVIQ 75
Cdd:pfam01408   1 IRVGIIGAGKIGSKHARALNAsqpGAELVAILDPNSERAEAVAESFGVEVYSDLEELlnDPEIDAVIVATPNGLHYDLAI 80


                  ..
gi 2158796580  76 EI 77
Cdd:pfam01408  81 AA 82
PRK07502 PRK07502
prephenate/arogenate dehydrogenase family protein;
2-100 7.21e-06

prephenate/arogenate dehydrogenase family protein;


Pssm-ID: 236034 [Multi-domain]  Cd Length: 307  Bit Score: 46.12  E-value: 7.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   2 RIGLIGAGRVAHHLAHVLNAQH---QIVqIYSRS---LDKAQDL--AAQVGAEAIAEVEqlhsDLDLLIIAVSDQAIAQV 73
Cdd:PRK07502    8 RVALIGIGLIGSSLARAIRRLGlagEIV-GADRSaetRARARELglGDRVTTSAAEAVK----GADLVILCVPVGASGAV 82

                          90       100
                  ....*....|....*....|....*..
gi 2158796580  74 IQEIHHDLNHVLIVHTSGSTKLDVLQQ 100
Cdd:PRK07502   83 AAEIAPHLKPGAIVTDVGSVKASVIAA 109
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 1-99 7.37e-06

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 46.10  E-value: 7.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   1 MRIGLIGAGRVAHHLAH------VLNAQHQIVQIYSRSldKAQDLAAQVGAEAIAEVEQLHSDLDLLIIAVSDQAIAQVI 74
Cdd:PLN02688    1 FRVGFIGAGKMAEAIARglvasgVVPPSRISTADDSNP--ARRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDVL 78

                          90       100
                  ....*....|....*....|....*..
gi 2158796580  75 QEIHHDL--NHVLIVHTSGsTKLDVLQ 99
Cdd:PLN02688   79 TELRPLLskDKLLVSVAAG-ITLADLQ 104
Rossmann-like pfam10727
Rossmann-like domain; This family of proteins contain a Rossmann-like domain.
 3-99 2.30e-05

Rossmann-like domain; This family of proteins contain a Rossmann-like domain.


Pssm-ID: 287672 [Multi-domain]  Cd Length: 127  Bit Score: 42.93  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   3 IGLIGAGRVAHHLAHVL-NAQHQIVQIYSRSLDKAQDLAAQVGAEAIAEVEQLHSDLDLLIIAVSDQAIAQVIQEIHHDL 81
Cdd:pfam10727  13 VGIISAGRVGTALGAALeRAGHVVVGISAISAASRERAERRLPDTPVLPVPDVAARAELLLLAVPDAELPGLVEGLAATG 92

                          90       100
                  ....*....|....*....|.
gi 2158796580  82 N---HVLIVHTSGSTKLDVLQ 99
Cdd:pfam10727  93 AvraGTIVAHTSGANGVGILA 113
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 5-66 7.68e-05

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 43.25  E-value: 7.68e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2158796580   5 LIGAGR----VAHHLAHvLNAQHqiVQIYSRSLDKAQDLAAQVGAEAI--AEVEQLHSDLDLLIIAVS 66
Cdd:PRK00045  187 VIGAGEmgelVAKHLAE-KGVRK--ITVANRTLERAEELAEEFGGEAIplDELPEALAEADIVISSTG 251
Shikimate_DH pfam01488
Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate ...
 2-66 9.97e-05

Shikimate / quinate 5-dehydrogenase; This family contains both shikimate and quinate dehydrogenases. Shikimate 5-dehydrogenase catalyzes the conversion of shikimate to 5-dehydroshikimate. This reaction is part of the shikimate pathway which is involved in the biosynthesis of aromatic amino acids. Quinate 5-dehydrogenase catalyzes the conversion of quinate to 5-dehydroquinate. This reaction is part of the quinate pathway where quinic acid is exploited as a source of carbon in prokaryotes and microbial eukaryotes. Both the shikimate and quinate pathways share two common pathway metabolites 3-dehydroquinate and dehydroshikimate.


Pssm-ID: 460229 [Multi-domain]  Cd Length: 136  Bit Score: 41.02  E-value: 9.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2158796580   2 RIGLIGAGRVAHHLA-HVLNAQHQIVQIYSRSLDKAQDLAAQVGAEAIAEVEQLHSDL---DLLIIAVS 66
Cdd:pfam01488  14 KVLLIGAGEMGELVAkHLLAKGAKEVTIANRTIERAQELAEKFGGVEALPLDDLKEYLaeaDIVISATS 82
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-109 1.07e-04

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 42.42  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   1 MRIGLIGAGRVAHHLAHVLNAQHQIVQI--YSRS---LDKAQDLaaQVGAEAIAEVEQLHSDLDLLIIAVSDQAIAQVIQ 75
Cdd:COG0287     2 MRIAIIGLGLIGGSLALALKRAGLAHEVvgVDRSpetLERALEL--GVIDRAATDLEEAVADADLVVLAVPVGATIEVLA 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2158796580  76 EIHHDLNHVLIVHTSGSTKLDVLQ--QHHARSGVFY 109
Cdd:COG0287    80 ELAPHLKPGAIVTDVGSVKGAVVEaaEALLPDGVRF 115
NAD_bind_Glutamyl_tRNA_reduct cd05213
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ...
 2-77 2.72e-04

NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133452 [Multi-domain]  Cd Length: 311  Bit Score: 41.48  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   2 RIGLIGAGR----VAHHLAhvlNAQHQIVQIYSRSLDKAQDLAAQVGAEAI--AEVEQLHSDLDLLIIAVSDQAIAQVIQ 75
Cdd:cd05213   180 KVLVIGAGEmgelAAKHLA---AKGVAEITIANRTYERAEELAKELGGNAVplDELLELLNEADVVISATGAPHYAKIVE 256


                  ..
gi 2158796580  76 EI 77
Cdd:cd05213   257 RA 258
HemA COG0373
Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part ...
 2-66 6.33e-04

Glutamyl-tRNA reductase [Coenzyme transport and metabolism]; Glutamyl-tRNA reductase is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440142 [Multi-domain]  Cd Length: 425  Bit Score: 40.48  E-value: 6.33e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2158796580   2 RIGLIGAGR----VAHHLAHvlnaqHQIVQIY--SRSLDKAQDLAAQVGAEAI--AEVEQLHSDLDLLIIAVS 66
Cdd:COG0373   184 TVLVIGAGEmgelAARHLAA-----KGVKRITvaNRTLERAEELAEEFGGEAVplEELPEALAEADIVISSTG 251
AroE COG0169
Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is ...
 7-62 2.08e-03

Shikimate 5-dehydrogenase [Amino acid transport and metabolism]; Shikimate 5-dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439939 [Multi-domain]  Cd Length: 270  Bit Score: 38.58  E-value: 2.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   7 GAGR-VAHHLAHvLNAQHqiVQIYSRSLDKAQDLAAQVGAEAIAeVEQLHSDL---DLLI 62
Cdd:COG0169   131 GAARaVAAALAE-AGAAE--ITIVNRTPERAEALAARLGVRAVP-LDDLAAALagaDLVI 186
PRK14619 PRK14619
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
 1-77 2.67e-03

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237771 [Multi-domain]  Cd Length: 308  Bit Score: 38.43  E-value: 2.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2158796580   1 MRIGLIGAGRVAHHLAHVLNAQHQIVQIYSRSldKAQDLAAQVGaeaiaeveqlhsDLDLLIIAVSDQAIAQVIQEI 77
Cdd:PRK14619    5 KTIAILGAGAWGSTLAGLASANGHRVRVWSRR--SGLSLAAVLA------------DADVIVSAVSMKGVRPVAEQV 67
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 2-80 2.77e-03

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 38.32  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   2 RIGLIGAGRVAHHLAHVLNAQHQIVQIYSRSlDKAQDLAAQVGAE-AIAEVEQLHSDLDLLII-AVSDQAIAQ------- 72
Cdd:cd08298   170 RLGLYGFGASAHLALQIARYQGAEVFAFTRS-GEHQELARELGADwAGDSDDLPPEPLDAAIIfAPVGALVPAalravkk 248

                          90
                  ....*....|..
gi 2158796580  73 ----VIQEIHHD 80
Cdd:cd08298   249 ggrvVLAGIHMS 260
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
1-59 4.18e-03

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 37.81  E-value: 4.18e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   1 MRIGLIGAGRVAHHLA-HVLNAQHQIVqIYSRSLDKAQDLAAQvGAEAIAEVEQLHSDLD 59
Cdd:PRK09599    1 MQLGMIGLGRMGGNMArRLLRGGHEVV-GYDRNPEAVEALAEE-GATGADSLEELVAKLP 58
TraI_TIGR TIGR02760
conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome ...
 15-138 5.34e-03

conjugative transfer relaxase protein TraI; This protein is a component of the relaxosome complex. In the process of conjugative plasmid transfer the realaxosome binds to the plasmid at the oriT (origin of transfer) site. The relaxase protein TraI mediates the single-strand nicking and ATP-dependent unwinding (relaxation, helicase activity) of the plasmid molecule. These two activities reside in separate domains of the protein.


Pssm-ID: 274285 [Multi-domain]  Cd Length: 1960  Bit Score: 37.96  E-value: 5.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158796580   15 LAHVLNAQHQIVQIYSRSLDKAQDLA--AQVGAEAIAEVEQLHSDLDLLIIAVSDQAiaqviqeIHHDLNHVLIVHTSGS 92
Cdd:TIGR02760  833 LLNSLNRSASRVDLFTDLDEKAQRYLekTRGIPSAIVVVDQKQHLPDAVTTNNTDKS-------LEMDISDTLHALEAKA 905

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2158796580   93 tkldvlQQHHARSGVFYPLQTFSlEREIDWTETPLFIEA-AFAEDQQ 138
Cdd:TIGR02760  906 ------KDGKNSIALQYALEKVS-EKEAAFKQKELVTEAyVFAFEET 945
 
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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