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Conserved domains on  [gi|496264774|ref|WP_008978159|]
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pyrroline-5-carboxylate reductase [Longicatena caecimuris]

Protein Classification

pyrroline-5-carboxylate reductase family protein( domain architecture ID 11417420)

pyrroline-5-carboxylate reductase family protein similar to pyrroline-5-carboxylate reductase that catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline

CATH:  1.10.3730.10|3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0004735|GO:0055129

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-266 3.44e-118

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: 338.96  E-value: 3.44e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   1 MKTIGFIGCGNMGKAMVEGiMKAQLVDGDHMIVSNQHPEKLETLSRTYDLYIS-DNETVACNADILFLAVKPHMYGKIIE 79
Cdd:COG0345    2 SMKIGFIGAGNMGSAIIKG-LLKSGVPPEDIIVSDRSPERLEALAERYGVRVTtDNAEAAAQADVVVLAVKPQDLAEVLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  80 EIREHVKPNAIMVNIAAGVTLADLYAMFHRKVKAVKAMPNTPAFVGEAMSALAFGEMMSKDDKEDIIDIFESFGQCAEVQ 159
Cdd:COG0345   81 ELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774 160 ESMMEAVTVVSGSSPAYMFMILEAMADEAVLEGMPRKDAYKFAAQAMLGSAKMLLETGKHPGELKDMVCSPGGTTIEAVM 239
Cdd:COG0345  161 EELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLK 240

                        250       260
                 ....*....|....*....|....*..
gi 496264774 240 KMEEKGLRSAIMEGMRACADKSRKMTK 266
Cdd:COG0345  241 VLEEGGLRAAVIEAVEAAAERSKELGK 267
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-266 3.44e-118

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: 338.96  E-value: 3.44e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   1 MKTIGFIGCGNMGKAMVEGiMKAQLVDGDHMIVSNQHPEKLETLSRTYDLYIS-DNETVACNADILFLAVKPHMYGKIIE 79
Cdd:COG0345    2 SMKIGFIGAGNMGSAIIKG-LLKSGVPPEDIIVSDRSPERLEALAERYGVRVTtDNAEAAAQADVVVLAVKPQDLAEVLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  80 EIREHVKPNAIMVNIAAGVTLADLYAMFHRKVKAVKAMPNTPAFVGEAMSALAFGEMMSKDDKEDIIDIFESFGQCAEVQ 159
Cdd:COG0345   81 ELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774 160 ESMMEAVTVVSGSSPAYMFMILEAMADEAVLEGMPRKDAYKFAAQAMLGSAKMLLETGKHPGELKDMVCSPGGTTIEAVM 239
Cdd:COG0345  161 EELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLK 240

                        250       260
                 ....*....|....*....|....*..
gi 496264774 240 KMEEKGLRSAIMEGMRACADKSRKMTK 266
Cdd:COG0345  241 VLEEGGLRAAVIEAVEAAAERSKELGK 267
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-267 2.20e-111

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 321.71  E-value: 2.20e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   1 MKTIGFIGCGNMGKAMVEGiMKAQLVDGDHMIVSNQHPEKLETLSRTYDLYI-SDNETVACNADILFLAVKPHMYGKIIE 79
Cdd:PRK11880   2 MKKIGFIGGGNMASAIIGG-LLASGVPAKDIIVSDPSPEKRAALAEEYGVRAaTDNQEAAQEADVVVLAVKPQVMEEVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  80 EIREHVKPnaIMVNIAAGVTLADLYAMFHRKVKAVKAMPNTPAFVGEAMSALAFGEMMSKDDKEDIIDIFESFGQCAEV- 158
Cdd:PRK11880  81 ELKGQLDK--LVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWVd 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774 159 QESMMEAVTVVSGSSPAYMFMILEAMADEAVLEGMPRKDAYKFAAQAMLGSAKMLLETGKHPGELKDMVCSPGGTTIEAV 238
Cdd:PRK11880 159 DEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAAL 238

                        250       260
                 ....*....|....*....|....*....
gi 496264774 239 MKMEEKGLRSAIMEGMRACADKSRKMTKK 267
Cdd:PRK11880 239 RVLEEKGLRAAVIEAVQAAAKRSKELGKE 267
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 20-263 7.69e-89

pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 272911 [Multi-domain]  Cd Length: 245  Bit Score: 263.74  E-value: 7.69e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   20 IMKAQLVDGDHMIVSNQHPEKLETLSRTYD-LYISDNETVACNADILFLAVKPHMYGKIIEEIREHVKPNAIMVNIAAGV 98
Cdd:TIGR00112   1 LLKAGALAPYDIYVINRSPEKLAALAKELGiVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   99 TLADLYAMFHRKVKAVKAMPNTPAFVGEAMSALAFGEMMSKDDKEDIIDIFESFGQCAEVQESMMEAVTVVSGSSPAYMF 178
Cdd:TIGR00112  81 TLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  179 MILEAMADEAVLEGMPRKDAYKFAAQAMLGSAKMLLETGKHPGELKDMVCSPGGTTIEAVMKMEEKGLRSAIMEGMRACA 258
Cdd:TIGR00112 161 LFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAV 240


                  ....*
gi 496264774  259 DKSRK 263
Cdd:TIGR00112 241 RRSRE 245
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 160-263 1.19e-51

Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of two domains, an N-terminal catalytic domain (pfam03807) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 464294 [Multi-domain]  Cd Length: 104  Bit Score: 164.11  E-value: 1.19e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  160 ESMMEAVTVVSGSSPAYMFMILEAMADEAVLEGMPRKDAYKFAAQAMLGSAKMLLETGKHPGELKDMVCSPGGTTIEAVM 239
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 496264774  240 KMEEKGLRSAIMEGMRACADKSRK 263
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKE 104
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 2-116 5.98e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 40.38  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   2 KTIGFIGCGNMGKAMVEgIMKAQLvdGDHMIVSNqhPEKLETLSRTYDLYISDNETVACNADI--LFLAVKPHMYGKIIE 79
Cdd:cd12177  148 KTVGIIGYGNIGSRVAE-ILKEGF--NAKVLAYD--PYVSEEVIKKKGAKPVSLEELLAESDIisLHAPLTEETYHMINE 222

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 496264774  80 EIREHVKPNAIMVNIAAGvTLADLYAMfhrkVKAVKA 116
Cdd:cd12177  223 KAFSKMKKGVILVNTARG-ELIDEEAL----IEALKS 254
 
Name Accession Description Interval E-value
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-266 3.44e-118

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: 338.96  E-value: 3.44e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   1 MKTIGFIGCGNMGKAMVEGiMKAQLVDGDHMIVSNQHPEKLETLSRTYDLYIS-DNETVACNADILFLAVKPHMYGKIIE 79
Cdd:COG0345    2 SMKIGFIGAGNMGSAIIKG-LLKSGVPPEDIIVSDRSPERLEALAERYGVRVTtDNAEAAAQADVVVLAVKPQDLAEVLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  80 EIREHVKPNAIMVNIAAGVTLADLYAMFHRKVKAVKAMPNTPAFVGEAMSALAFGEMMSKDDKEDIIDIFESFGQCAEVQ 159
Cdd:COG0345   81 ELAPLLDPDKLVISIAAGVTLATLEEALGGGAPVVRAMPNTPALVGEGVTALAAGEAVSEEDRELVEALFSAVGKVVWVD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774 160 ESMMEAVTVVSGSSPAYMFMILEAMADEAVLEGMPRKDAYKFAAQAMLGSAKMLLETGKHPGELKDMVCSPGGTTIEAVM 239
Cdd:COG0345  161 EELMDAVTALSGSGPAYVFLFIEAMADAGVALGLPRETARELAAQTVLGAAKLLLESGEHPAELRDRVTSPGGTTIAGLK 240

                        250       260
                 ....*....|....*....|....*..
gi 496264774 240 KMEEKGLRSAIMEGMRACADKSRKMTK 266
Cdd:COG0345  241 VLEEGGLRAAVIEAVEAAAERSKELGK 267
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-267 2.20e-111

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 321.71  E-value: 2.20e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   1 MKTIGFIGCGNMGKAMVEGiMKAQLVDGDHMIVSNQHPEKLETLSRTYDLYI-SDNETVACNADILFLAVKPHMYGKIIE 79
Cdd:PRK11880   2 MKKIGFIGGGNMASAIIGG-LLASGVPAKDIIVSDPSPEKRAALAEEYGVRAaTDNQEAAQEADVVVLAVKPQVMEEVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  80 EIREHVKPnaIMVNIAAGVTLADLYAMFHRKVKAVKAMPNTPAFVGEAMSALAFGEMMSKDDKEDIIDIFESFGQCAEV- 158
Cdd:PRK11880  81 ELKGQLDK--LVVSIAAGVTLARLERLLGADLPVVRAMPNTPALVGAGMTALTANALVSAEDRELVENLLSAFGKVVWVd 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774 159 QESMMEAVTVVSGSSPAYMFMILEAMADEAVLEGMPRKDAYKFAAQAMLGSAKMLLETGKHPGELKDMVCSPGGTTIEAV 238
Cdd:PRK11880 159 DEKQMDAVTAVSGSGPAYVFLFIEALADAGVKLGLPREQARKLAAQTVLGAAKLLLESGEHPAELRDNVTSPGGTTIAAL 238

                        250       260
                 ....*....|....*....|....*....
gi 496264774 239 MKMEEKGLRSAIMEGMRACADKSRKMTKK 267
Cdd:PRK11880 239 RVLEEKGLRAAVIEAVQAAAKRSKELGKE 267
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 2-266 3.02e-90

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 267.98  E-value: 3.02e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   2 KTIGFIGCGNMGKAMVEGIMKAQLVDGDHMIVSNQHPEKLETLSRTYDLYI-SDNETVACNADILFLAVKPHMYGKIIEE 80
Cdd:PLN02688   1 FRVGFIGAGKMAEAIARGLVASGVVPPSRISTADDSNPARRDVFQSLGVKTaASNTEVVKSSDVIILAVKPQVVKDVLTE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  81 IREHVKPNAIMVNIAAGVTLADL-YAMFHRKVkaVKAMPNTPAFVGEAMSALAFGEMMSKDDKEDIIDIFESFGQCAEVQ 159
Cdd:PLN02688  81 LRPLLSKDKLLVSVAAGITLADLqEWAGGRRV--VRVMPNTPCLVGEAASVMSLGPAATADDRDLVATLFGAVGKIWVVD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774 160 ESMMEAVTVVSGSSPAYMFMILEAMADEAVLEGMPRKDAYKFAAQAMLGSAKMLLETGKHPGELKDMVCSPGGTTIEAVM 239
Cdd:PLN02688 159 EKLLDAVTGLSGSGPAYIFLAIEALADGGVAAGLPRDVALSLAAQTVLGAAKMVLETGKHPGQLKDMVTSPGGTTIAGVH 238

                        250       260
                 ....*....|....*....|....*..
gi 496264774 240 KMEEKGLRSAIMEGMRACADKSRKMTK 266
Cdd:PLN02688 239 ELEKGGFRAALMNAVVAAAKRSRELSK 265
proC TIGR00112
pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline ...
 20-263 7.69e-89

pyrroline-5-carboxylate reductase; This enzyme catalyzes the final step in proline biosynthesis. Among the four paralogs in Bacillus subtilis (proG, proH, proI, and comER), ComER is the most divergent and does not prevent proline auxotrophy from mutation of the other three. It is excluded from the seed and scores between the trusted and noise cutoffs. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 272911 [Multi-domain]  Cd Length: 245  Bit Score: 263.74  E-value: 7.69e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   20 IMKAQLVDGDHMIVSNQHPEKLETLSRTYD-LYISDNETVACNADILFLAVKPHMYGKIIEEIREHVKPNAIMVNIAAGV 98
Cdd:TIGR00112   1 LLKAGALAPYDIYVINRSPEKLAALAKELGiVASSDAQEAVKEADVVFLAVKPQDLEEVLSELKSEKGKDKLLISIAAGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   99 TLADLYAMFHRKVKAVKAMPNTPAFVGEAMSALAFGEMMSKDDKEDIIDIFESFGQCAEVQESMMEAVTVVSGSSPAYMF 178
Cdd:TIGR00112  81 TLEKLSQLLGGTRRVVRVMPNTPAKVGAGVTAIAANANVSEEDRALALALFKAVGSVVELPEALMDAVTALSGSGPAYVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  179 MILEAMADEAVLEGMPRKDAYKFAAQAMLGSAKMLLETGKHPGELKDMVCSPGGTTIEAVMKMEEKGLRSAIMEGMRACA 258
Cdd:TIGR00112 161 LFIEALADAGVKQGLPRELALELAAQTVKGAAKLLEESGEHPALLKDQVTSPGGTTIAGLAVLEEKGVRGAVIEAIEAAV 240


                  ....*
gi 496264774  259 DKSRK 263
Cdd:TIGR00112 241 RRSRE 245
PTZ00431 PTZ00431
pyrroline carboxylate reductase; Provisional
 4-264 6.88e-52

pyrroline carboxylate reductase; Provisional


Pssm-ID: 173621 [Multi-domain]  Cd Length: 260  Bit Score: 170.13  E-value: 6.88e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   4 IGFIGCGNMGKAMVEGIMKAQLVDGDHMIVSNqhPEKLETLSrtydLYISDNETVACNADILFLAVKPHMYGKIIEEIRE 83
Cdd:PTZ00431   6 VGFIGLGKMGSALAYGIENSNIIGKENIYYHT--PSKKNTPF----VYLQSNEELAKTCDIIVLAVKPDLAGKVLLEIKP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  84 HVKPNaIMVNIAAGVTLADLYAMFHRKVKAVKAMPNTPAFVGEAMSALAFGEMMSKDDKEDIIDIFESFGQCAEVQESMM 163
Cdd:PTZ00431  80 YLGSK-LLISICGGLNLKTLEEMVGVEAKIVRVMPNTPSLVGQGSLVFCANNNVDSTDKKKVIDIFSACGIIQEIKEKDM 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774 164 EAVTVVSGSSPAYMFMILEAMADEAVLEGMPRKDAYKFAAQAMLGSAKMLLETGKHPGELKDMVCSPGGTTIEAVMKMEE 243
Cdd:PTZ00431 159 DIATAISGCGPAYVFLFIESLIDAGVKNGLNRDVSKNLVLQTILGSVHMVKASDQPVQQLKDDVCSPGGITIVGLYTLEK 238

                        250       260
                 ....*....|....*....|.
gi 496264774 244 KGLRSAIMEGMRACADKSRKM 264
Cdd:PTZ00431 239 HAFKYTVMDAVESACQKSKSM 259
P5CR_dimer pfam14748
Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of ...
 160-263 1.19e-51

Pyrroline-5-carboxylate reductase dimerization; Pyrroline-5-carboxylate reductase consists of two domains, an N-terminal catalytic domain (pfam03807) and a C-terminal dimerization domain. This is the dimerization domain.


Pssm-ID: 464294 [Multi-domain]  Cd Length: 104  Bit Score: 164.11  E-value: 1.19e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  160 ESMMEAVTVVSGSSPAYMFMILEAMADEAVLEGMPRKDAYKFAAQAMLGSAKMLLETGKHPGELKDMVCSPGGTTIEAVM 239
Cdd:pfam14748   1 ESLMDAVTALSGSGPAYVFLFIEALADAGVAMGLPREEARELAAQTVLGAAKLLLTSGEHPAELRDKVTSPGGTTIAGLA 80

                          90       100
                  ....*....|....*....|....
gi 496264774  240 KMEEKGLRSAIMEGMRACADKSRK 263
Cdd:pfam14748  81 VLEEGGFRGAVIEAVEAATKRAKE 104
PRK07679 PRK07679
pyrroline-5-carboxylate reductase; Reviewed
 1-266 2.73e-51

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 181079 [Multi-domain]  Cd Length: 279  Bit Score: 169.18  E-value: 2.73e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   1 MKTIGFIGCGNMGKAMVEGIMKAQLVDGDHMIVSN-QHPEKLETLSRTYDLYISDNETVAC-NADILFLAVKPHMYGKII 78
Cdd:PRK07679   3 IQNISFLGAGSIAEAIIGGLLHANVVKGEQITVSNrSNETRLQELHQKYGVKGTHNKKELLtDANILFLAMKPKDVAEAL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  79 EEIREHVKPNAIMVNIAAGVTLADLYAMFHRKVKAVKAMPNTPAFVGEAMSALAFGEMMSKDDKEDIIDIFESFGQCAEV 158
Cdd:PRK07679  83 IPFKEYIHNNQLIISLLAGVSTHSIRNLLQKDVPIIRAMPNTSAAILKSATAISPSKHATAEHIQTAKALFETIGLVSVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774 159 QESMMEAVTVVSGSSPAYMFMILEAMADEAVLEGMPRKDAYKFAAQAMLGSAKMLLETGKHPGELKDMVCSPGGTTIEAV 238
Cdd:PRK07679 163 EEEDMHAVTALSGSGPAYIYYVVEAMEKAAKKIGLKEDVAKSLILQTMIGAAEMLKASEKHPSILRKEITSPGGTTEAGI 242

                        250       260
                 ....*....|....*....|....*...
gi 496264774 239 MKMEEKGLRSAIMEGMRACADKSRKMTK 266
Cdd:PRK07679 243 EVLQEHRFQQALISCITQATQRSHNLGK 270
PRK07680 PRK07680
late competence protein ComER; Validated
 1-243 2.43e-31

late competence protein ComER; Validated


Pssm-ID: 181080 [Multi-domain]  Cd Length: 273  Bit Score: 117.00  E-value: 2.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   1 MKtIGFIGCGNMGKAMVEGIMKAQLVDGDHMIVSNQHPEKLETLSRTY-DLYISD-NETVACNADILFLAVKPHMYGKII 78
Cdd:PRK07680   1 MN-IGFIGTGNMGTILIEAFLESGAVKPSQLTITNRTPAKAYHIKERYpGIHVAKtIEEVISQSDLIFICVKPLDIYPLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  79 EEIREHVKPNAIMVNIAAGVTLADLYAMFHRKVkaVKAMPNTPAFVGEAMSALAFGEMMSKDDKEDIIDIFESFGQCAEV 158
Cdd:PRK07680  80 QKLAPHLTDEHCLVSITSPISVEQLETLVPCQV--ARIIPSITNRALSGASLFTFGSRCSEEDQQKLERLFSNISTPLVI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774 159 QESMMEAVTVVSGSSPAYMFMILEAMADEAVLE-GMPRKDAYKFAAQAMLGSAKMLLETGKHPGELKDMVCSPGGTTIEA 237
Cdd:PRK07680 158 EEDITRVSSDIVSCGPAFFSYLLQRFIDAAVEEtNISKEEATTLASEMLIGMGKLLEKGLYTLPTLQEKVCVKGGITGEG 237


                 ....*.
gi 496264774 238 VMKMEE 243
Cdd:PRK07680 238 IKVLEE 243
PRK06928 PRK06928
pyrroline-5-carboxylate reductase; Reviewed
 1-238 5.59e-26

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235888 [Multi-domain]  Cd Length: 277  Bit Score: 102.92  E-value: 5.59e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   1 MKTIGFIGCGNMGKAMVEGIMKAQLVDGDHMIV-SNQHPEKLETLsrtYDLY-----ISDNETVACNADILFLAVKPHMY 74
Cdd:PRK06928   1 MEKIGFIGYGSMADMIATKLLETEVATPEEIILySSSKNEHFNQL---YDKYptvelADNEAEIFTKCDHSFICVPPLAV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  75 GKIIEEIREHVKPNAIMVNIAAGVTLADLYAMfHRKVKAVKAMPNTPAFVGEAMSALAFGEMMSKDDKEDIIDIFESFGQ 154
Cdd:PRK06928  78 LPLLKDCAPVLTPDRHVVSIAAGVSLDDLLEI-TPGLQVSRLIPSLTSAVGVGTSLVAHAETVNEANKSRLEETLSHFSH 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774 155 CAEVQESMMEAVTVVSGSSPAYMFMILEAMADEAVLEG-MPRKDAYKFAAQAMLGSAKMLLETGKHPGELKDMVCSPGGT 233
Cdd:PRK06928 157 VMTIREENMDIASNLTSSSPGFIAAIFEEFAEAAVRNSsLSDEEAFQFLNFALAGTGKLLVEEDYTFSGTIERVATKGGI 236


                 ....*
gi 496264774 234 TIEAV 238
Cdd:PRK06928 237 TAEGA 241
PRK06476 PRK06476
pyrroline-5-carboxylate reductase; Reviewed
 1-249 1.53e-15

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 235812 [Multi-domain]  Cd Length: 258  Bit Score: 73.90  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   1 MKtIGFIGCGNMGKAMVEGIMkAQLVDGDHMIVSNQHPEKLETLSRTYDLYI--SDNETVACNADILFLAVKPHMYGKII 78
Cdd:PRK06476   1 MK-IGFIGTGAITEAMVTGLL-TSPADVSEIIVSPRNAQIAARLAERFPKVRiaKDNQAVVDRSDVVFLAVRPQIAEEVL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774  79 EEIRehVKPNAIMVNIAAGVTLADLYAMFHRKVKAVKAMPnTPaFVGEAMSALAFgemmsKDDKEDIIDIFESFGQCAEV 158
Cdd:PRK06476  79 RALR--FRPGQTVISVIAATDRAALLEWIGHDVKLVRAIP-LP-FVAERKGVTAI-----YPPDPFVAALFDALGTAVEC 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774 159 Q-ESMMEAVTVVSGSSPAYmFMILEAMADEAVLEGMPRKDAYKFAAQAMLGSAKMLLETGKHP-GELKDMVCSPGGTTiE 236
Cdd:PRK06476 150 DsEEEYDLLAAASALMATY-FGILETATGWLEEQGLKRQKARAYLAPLFASLAQDAVRSTKTDfSALSREFSTKGGLN-E 227

                        250
                 ....*....|....
gi 496264774 237 AVMK-MEEKGLRSA 249
Cdd:PRK06476 228 QVLNdFSRQGGYAA 241
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
5-97 6.75e-15

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 68.41  E-value: 6.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774    5 GFIGCGNMGKAMVEGIMKAqlvdGDH--MIVSNQHPEKLETLSRTY--DLYISDNETVACNADILFLAVKPHMYGKIIEE 80
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAA----GPHevVVANSRNPEKAEELAEEYgvGATAVDNEEAAEEADVVFLAVKPEDAPDVLSE 76

                          90
                  ....*....|....*..
gi 496264774   81 IReHVKPNAIMVNIAAG 97
Cdd:pfam03807  77 LS-DLLKGKIVISIAAG 92
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
4-86 1.80e-06

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 47.47  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   4 IGFIGCGNMGKAMVEGIMKAqlvdGDHMIVSNQHPEKLETLSRTYDLYIS--DNETVACNADILFLAVKPHMYGKIIEEI 81
Cdd:COG2085    1 IGIIGTGNIGSALARRLAAA----GHEVVIGSRDPEKAAALAAELGPGARagTNAEAAAAADVVVLAVPYEAVPDVLESL 76


                 ....*
gi 496264774  82 REHVK 86
Cdd:COG2085   77 GDALA 81
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-92 1.63e-05

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


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 45.19  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   1 MKTIGFIGCGNMGKAMVEGIMKAQL-VDGdhmiVSNQHPEKLETLS-RTYDLYISDNETVACNADILFLAVKPHMYGKII 78
Cdd:COG5495    3 RMKIGIIGAGRVGTALAAALRAAGHeVVG----VYSRSPASAERAAaLLGAVPALDLEELAAEADLVLLAVPDDAIAEVA 78

                         90
                 ....*....|....*.
gi 496264774  79 EEIRE--HVKPNAIMV 92
Cdd:COG5495   79 AGLAAagALRPGQLVV 94
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 3-92 3.18e-04

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 40.15  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774    3 TIGFIGCGNMGKAMVEGIMKAqlvdGDHMIVSNQHPEKLETLSRTYDLYISDNETVACNADILFLAVKphmYGKIIEE-- 80
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKA----GYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVP---AGAAVDAvi 73

                          90
                  ....*....|....*.
gi 496264774   81 ----IREHVKPNAIMV 92
Cdd:pfam03446  74 fgegLLPGLKPGDIII 89
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 2-105 3.46e-04

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 40.17  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774    2 KTIGFIGCGNMGKAmVEGIMKAQlvdGDHMIVSNQHPEKLETLSRTYDLYISDNETVAcNADILFLAV--KPHMYGKIIE 79
Cdd:pfam02826  37 KTVGIIGLGRIGRA-VAKRLKAF---GMKVIAYDRYPKPEEEEEELGARYVSLDELLA-ESDVVSLHLplTPETRHLINA 111

                          90       100
                  ....*....|....*....|....*...
gi 496264774   80 EIREHVKPNAIMVNIAAG--VTLADLYA 105
Cdd:pfam02826 112 ERLALMKPGAILINTARGglVDEDALIA 139
2-Hacid_dh_12 cd12177
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ...
 2-116 5.98e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240654 [Multi-domain]  Cd Length: 321  Bit Score: 40.38  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   2 KTIGFIGCGNMGKAMVEgIMKAQLvdGDHMIVSNqhPEKLETLSRTYDLYISDNETVACNADI--LFLAVKPHMYGKIIE 79
Cdd:cd12177  148 KTVGIIGYGNIGSRVAE-ILKEGF--NAKVLAYD--PYVSEEVIKKKGAKPVSLEELLAESDIisLHAPLTEETYHMINE 222

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 496264774  80 EIREHVKPNAIMVNIAAGvTLADLYAMfhrkVKAVKA 116
Cdd:cd12177  223 KAFSKMKKGVILVNTARG-ELIDEEAL----IEALKS 254
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-44 7.44e-04

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 40.10  E-value: 7.44e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 496264774   1 MKTIGFIGCGNMGKAMVEGIMKAqlvdGDHMIVSNQHPEKLETL 44
Cdd:COG2084    1 MMKVGFIGLGAMGAPMARNLLKA----GHEVTVWNRTPAKAEAL 40
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 2-105 1.77e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 39.15  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   2 KTIGFIGCGNMGKAmVEGIMKAQlvdGDHMIVSNQHPEKLETLSrtYDLYISDNETVACNADILFLAV--KPHMYGKIIE 79
Cdd:cd12165  138 KTVGILGYGHIGRE-IARLLKAF---GMRVIGVSRSPKEDEGAD--FVGTLSDLDEALEQADVVVVALplTKQTRGLIGA 211

                         90       100
                 ....*....|....*....|....*...
gi 496264774  80 EIREHVKPNAIMVNIAAGVTL--ADLYA 105
Cdd:cd12165  212 AELAAMKPGAILVNVGRGPVVdeEALYE 239
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-96 1.92e-03

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 38.88  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   1 MKTIGFIGCGNMGKAMVEGIMKAqlvdGDHMIVSNQHPEKLETLSRTYDLYISDNETVACNADILF--LAVKPHMYGKII 78
Cdd:PRK11559   2 TMKVGFIGLGIMGKPMSKNLLKA----GYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIItmLPNSPHVKEVAL 77

                         90       100
                 ....*....|....*....|
gi 496264774  79 EE--IREHVKPNAIMVNIAA 96
Cdd:PRK11559  78 GEngIIEGAKPGTVVIDMSS 97
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-90 3.01e-03

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: 38.18  E-value: 3.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496264774   1 MKTIGFIGCGNMGKAMVEGIMKAQLVDgdHMIVSNQHPEKLET-LSRTY-DLYISDNETVACNADILFLAVKPHMYGKII 78
Cdd:COG0287    1 FMRIAIIGLGLIGGSLALALKRAGLAH--EVVGVDRSPETLERaLELGViDRAATDLEEAVADADLVVLAVPVGATIEVL 78

                         90
                 ....*....|..
gi 496264774  79 EEIREHVKPNAI 90
Cdd:COG0287   79 AELAPHLKPGAI 90
 
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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