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PIG:MDHC

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Species (Taxon ID) Sus scrofa (Pig). (9823)
Gene Name(s) MDH1
Protein Name(s) Malate dehydrogenase, cytoplasmic

Cytosolic malate dehydrogenase

External Links
UniProt P11708
EMBL U44846
M29463
PIR JC4876
RefSeq NP_999039.1
UniGene Ssc.11103
PDB 4MDH
5MDH
PDBsum 4MDH
5MDH
ProteinModelPortal P11708
SMR P11708
BindingDB P11708
ChEMBL CHEMBL4048
PRIDE P11708
GeneID 396894
KEGG ssc:396894
CTD 4190
HOVERGEN HBG006340
InParanoid P11708
KO K00025
BioCyc MetaCyc:MONOMER-13033
SABIO-RK P11708
EvolutionaryTrace P11708
Proteomes UP000008227
GO GO:0005829
GO:0030060
GO:0044262
GO:0006108
GO:0006099
Gene3D 3.40.50.720
3.90.110.10
HAMAP MF_01517
InterPro IPR001557
IPR022383
IPR001236
IPR015955
IPR001252
IPR011274
IPR010945
IPR016040
PANTHER PTHR23382
Pfam PF02866
PF00056
PIRSF PIRSF000102
SUPFAM SSF56327
TIGRFAMs TIGR01759
TIGR01758
PROSITE PS00068

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0051287

NAD binding

PMID:10075524[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0030060

L-malate dehydrogenase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0262782
PANTHER:PTN000600336
RGD:3072
UniProtKB:P9WK13

F

Seeded From UniProt

complete

involved_in

GO:0006734

NADH metabolic process

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000600336
RGD:3072

P

Seeded From UniProt

complete

involved_in

GO:0006108

malate metabolic process

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000600336
RGD:3072

P

Seeded From UniProt

complete

involved_in

GO:0006107

oxaloacetate metabolic process

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000600336
RGD:3072

P

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000600336
UniProtKB:P9WK13

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0262782
PANTHER:PTN001157397
UniProtKB:P11708

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:3312200[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR015955

F

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR015955

P

Seeded From UniProt

complete

involved_in

GO:0006108

malate metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001252
InterPro:IPR010945
InterPro:IPR011274

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001236

F

Seeded From UniProt

complete

enables

GO:0016615

malate dehydrogenase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001252
InterPro:IPR010945

F

Seeded From UniProt

complete

enables

GO:0016616

oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001557
InterPro:IPR015955
InterPro:IPR022383

F

Seeded From UniProt

complete

involved_in

GO:0019752

carboxylic acid metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001557

P

Seeded From UniProt

complete

enables

GO:0030060

L-malate dehydrogenase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011274

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001236
InterPro:IPR001252
InterPro:IPR001557
InterPro:IPR010945
InterPro:IPR011274
InterPro:IPR015955
InterPro:IPR022383

P

Seeded From UniProt

complete

enables

GO:0030060

L-malate dehydrogenase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.1.1.37

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0006099

tricarboxylic acid cycle

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0816

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Chapman, AD et al. (1999) Structural basis of substrate specificity in malate dehydrogenases: crystal structure of a ternary complex of porcine cytoplasmic malate dehydrogenase, alpha-ketomalonate and tetrahydoNAD. J. Mol. Biol. 285 703-12 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 2.4 2.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. Joh, T et al. (1987) Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase. J. Biol. Chem. 262 15127-31 PubMed GONUTS page