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Conserved domains on  [gi|1376753608|gb|PTP48319|]
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malate synthase [Vibrio splendidus]

Protein Classification

aldolase/citrate lyase/malate synthase family protein; malate synthase( domain architecture ID 10013128)

aldolase/citrate lyase/malate synthase family protein; similar to 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) aldolase (HpcH/HpaI) that catalyzes the reversible retro-aldol cleavage of HKHD to pyruvate and succinic semialdehyde, and to malate synthase that catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA, which hydrolyzes to malate and CoA, in the glyoxylate cycle| malate synthase catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA, which hydrolyzes to malate and CoA, in the glyoxylate cycle

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08951 PRK08951
malate synthase; Provisional
 1-190 3.75e-108

malate synthase; Provisional


:

Pssm-ID: 181593 [Multi-domain]  Cd Length: 190  Bit Score: 307.33  E-value: 3.75e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376753608   1 MNMLTLDRTELHRNHSTFIAEAVFAVEMVKADKQLEKQKMAKQLLDTLFPLEAGSHEDAVSYEIDYRHVQVYFKNGEHTG 80
Cdd:PRK08951    1 MNMSTINSTQIQQNLNPFIAEAVFAVETVNAAQQEEKQAKAKQFLDRLFPLANGSHQDVSSYVVYYQHLLAFFADGSHSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376753608  81 LKRAKHFVAFTGDKSKPSAILFRDeSGTHVEVTIGARKGTGYLELVDIQDIQLETCTTFGQT-EASRSSGIRHWVSLVKG 159
Cdd:PRK08951   81 LRQPKQFVAFNGHKSEPSAILLKD-SGSHVELTFDRHGGTGSRDLANIEDIQLETCTTFSQEpTENRSTAMRHWISLLKG 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1376753608 160 DESGRPNASSEDKEFTAKNGEDYNLGFCFAI 190
Cdd:PRK08951  160 DESGRPAADQEDKEFTAKDGSDYQLKSCFSL 190
 
Name Accession Description Interval E-value
PRK08951 PRK08951
malate synthase; Provisional
 1-190 3.75e-108

malate synthase; Provisional


Pssm-ID: 181593 [Multi-domain]  Cd Length: 190  Bit Score: 307.33  E-value: 3.75e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376753608   1 MNMLTLDRTELHRNHSTFIAEAVFAVEMVKADKQLEKQKMAKQLLDTLFPLEAGSHEDAVSYEIDYRHVQVYFKNGEHTG 80
Cdd:PRK08951    1 MNMSTINSTQIQQNLNPFIAEAVFAVETVNAAQQEEKQAKAKQFLDRLFPLANGSHQDVSSYVVYYQHLLAFFADGSHSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376753608  81 LKRAKHFVAFTGDKSKPSAILFRDeSGTHVEVTIGARKGTGYLELVDIQDIQLETCTTFGQT-EASRSSGIRHWVSLVKG 159
Cdd:PRK08951   81 LRQPKQFVAFNGHKSEPSAILLKD-SGSHVELTFDRHGGTGSRDLANIEDIQLETCTTFSQEpTENRSTAMRHWISLLKG 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1376753608 160 DESGRPNASSEDKEFTAKNGEDYNLGFCFAI 190
Cdd:PRK08951  160 DESGRPAADQEDKEFTAKDGSDYQLKSCFSL 190
malate_synt_G cd00728
Malate synthase G (MSG), monomeric enzyme present in some bacteria. In general, malate ...
 38-160 2.89e-19

Malate synthase G (MSG), monomeric enzyme present in some bacteria. In general, malate synthase catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA , which hydrolyzes to malate and CoA. This reaction is part of the glyoxylate cycle, which allows certain organisms to derive their carbon requirements from two-carbon compounds, by bypassing the two carboxylation steps of the citric acid cycle.


Pssm-ID: 238370 [Multi-domain]  Cd Length: 712  Bit Score: 84.39  E-value: 2.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376753608  38 QKMAKQLLDTLFPLEAGSHEDAVSYEIDYRHVQVYFKNGEHTGLKRAKHFVAFTGDKSKPSAILFRDeSGTHVEVTIGAR 117
Cdd:cd00728   161 IAYARRFLDESVPLTNGSHADATGYKVVDGQLVVTLDDGKTTTLKDPAQFVGYRGDANAPSAVLLKH-NGLHIEIQIDRN 239

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1376753608 118 KGTGYLELVDIQDIQLETC-TTFGQTEAS--------RSSGIRHWVSLVKGD 160
Cdd:cd00728   240 HQIGKTDPAGVKDVVVEAAlTTIMDCEDSvaavdaedKVLVYRNWLGLMKGD 291
 
Name Accession Description Interval E-value
PRK08951 PRK08951
malate synthase; Provisional
 1-190 3.75e-108

malate synthase; Provisional


Pssm-ID: 181593 [Multi-domain]  Cd Length: 190  Bit Score: 307.33  E-value: 3.75e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376753608   1 MNMLTLDRTELHRNHSTFIAEAVFAVEMVKADKQLEKQKMAKQLLDTLFPLEAGSHEDAVSYEIDYRHVQVYFKNGEHTG 80
Cdd:PRK08951    1 MNMSTINSTQIQQNLNPFIAEAVFAVETVNAAQQEEKQAKAKQFLDRLFPLANGSHQDVSSYVVYYQHLLAFFADGSHSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376753608  81 LKRAKHFVAFTGDKSKPSAILFRDeSGTHVEVTIGARKGTGYLELVDIQDIQLETCTTFGQT-EASRSSGIRHWVSLVKG 159
Cdd:PRK08951   81 LRQPKQFVAFNGHKSEPSAILLKD-SGSHVELTFDRHGGTGSRDLANIEDIQLETCTTFSQEpTENRSTAMRHWISLLKG 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1376753608 160 DESGRPNASSEDKEFTAKNGEDYNLGFCFAI 190
Cdd:PRK08951  160 DESGRPAADQEDKEFTAKDGSDYQLKSCFSL 190
PRK02999 PRK02999
malate synthase G; Provisional
 41-184 2.07e-22

malate synthase G; Provisional


Pssm-ID: 235097 [Multi-domain]  Cd Length: 726  Bit Score: 93.70  E-value: 2.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376753608  41 AKQLLDTLFPLEAGSHEDAVSYEIDYRHVQVYFKNGEHTGLKRAKHFVAFTGDKSKPSAILFRDeSGTHVEVTIGARKGT 120
Cdd:PRK02999  172 ARAFLDEAAPLASGSHADVTGYAVEDGQLVVTLKDGSETGLADPAQFVGYQGDAAAPSAILLKN-NGLHIEIQIDRNHPI 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376753608 121 GYLELVDIQDIQLETC-TTFGQTEAS--------RSSGIRHWVSLVKGD-----ESG------RPNAsseDKEFTAKNGE 180
Cdd:PRK02999  251 GKTDPAGVKDVVLESAlTTIMDCEDSvaavdaedKVLVYRNWLGLMKGDlteefEKGgktftrRLNP---DREYTAPDGG 327


                  ....
gi 1376753608 181 DYNL 184
Cdd:PRK02999  328 ELTL 331
malate_synt_G cd00728
Malate synthase G (MSG), monomeric enzyme present in some bacteria. In general, malate ...
 38-160 2.89e-19

Malate synthase G (MSG), monomeric enzyme present in some bacteria. In general, malate synthase catalyzes the Claisen condensation of glyoxylate and acetyl-CoA to malyl-CoA , which hydrolyzes to malate and CoA. This reaction is part of the glyoxylate cycle, which allows certain organisms to derive their carbon requirements from two-carbon compounds, by bypassing the two carboxylation steps of the citric acid cycle.


Pssm-ID: 238370 [Multi-domain]  Cd Length: 712  Bit Score: 84.39  E-value: 2.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376753608  38 QKMAKQLLDTLFPLEAGSHEDAVSYEIDYRHVQVYFKNGEHTGLKRAKHFVAFTGDKSKPSAILFRDeSGTHVEVTIGAR 117
Cdd:cd00728   161 IAYARRFLDESVPLTNGSHADATGYKVVDGQLVVTLDDGKTTTLKDPAQFVGYRGDANAPSAVLLKH-NGLHIEIQIDRN 239

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1376753608 118 KGTGYLELVDIQDIQLETC-TTFGQTEAS--------RSSGIRHWVSLVKGD 160
Cdd:cd00728   240 HQIGKTDPAGVKDVVVEAAlTTIMDCEDSvaavdaedKVLVYRNWLGLMKGD 291
 
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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