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Database: UniProt/TrEMBL
Entry: A0A0M4SWY6_9GAMM
LinkDB: A0A0M4SWY6_9GAMM
Original site: A0A0M4SWY6_9GAMM 
ID   A0A0M4SWY6_9GAMM        Unreviewed;       327 AA.
AC   A0A0M4SWY6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-SEP-2017, entry version 15.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU004066, ECO:0000256|SAAS:SAAS00369716};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU004066, ECO:0000256|SAAS:SAAS00369716};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN   ORFNames=AOC03_04310 {ECO:0000313|EMBL:ALF59372.1};
OS   Psychrobacter urativorans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=45610 {ECO:0000313|EMBL:ALF59372.1};
RN   [1] {ECO:0000313|EMBL:ALF59372.1, ECO:0000313|Proteomes:UP000059847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R10.10B {ECO:0000313|EMBL:ALF59372.1,
RC   ECO:0000313|Proteomes:UP000059847};
RA   See-Too W.S., Chan K.G.;
RT   "Complete genome of Psychrobacter urativorans R10.10B.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate. {ECO:0000256|HAMAP-Rule:MF_01517,
CC       ECO:0000256|SAAS:SAAS00755561}.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC       {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU004066,
CC       ECO:0000256|SAAS:SAAS00369698}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01517}.
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DR   EMBL; CP012678; ALF59372.1; -; Genomic_DNA.
DR   RefSeq; WP_062533758.1; NZ_CP012678.1.
DR   EnsemblBacteria; ALF59372; ALF59372; AOC03_04310.
DR   KEGG; pur:AOC03_04310; -.
DR   KO; K00024; -.
DR   Proteomes; UP000059847; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01517; Malate_dehydrog_2; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR001252; Malate_DH_AS.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR23382; PTHR23382; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000059847};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU004066, ECO:0000313|EMBL:ALF59372.1};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN        5    152       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      156    322       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND      11     17       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   NP_BIND     129    131       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    187    187       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                1}.
FT   BINDING      92     92       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING      98     98       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     105    105       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     112    112       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     131    131       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
SQ   SEQUENCE   327 AA;  35132 MW;  10A7325A2E04192E CRC64;
     MKQPVRVAVT GAAGNISYAM LFRIASGEML GKDQPVILQL LEIAPALDAL KGVVMELEDC
     AFPLLAGIVQ TDDATVAFKD IDYALLVGSR PRGPGMERKD LLEANAAIFS AQGKALNDVA
     SRDVKVLVVG NPANTNAVIA QRNAPDLDPR NFTAMTRLDH NRAMAQLAGK TDSTVNDVKK
     MTIWGNHSST QYPDLTACTV KGKPALDLVD REWYEATYIP EVQQRGAAII KARGASSAAS
     AANAAIAHVR TWVMGTDEND WVSMGVYSNG EYGISKGLIY SFPCTCKDGD WAIVEGVDVS
     SAFSKEKMAA TEQELNEERD AVSHLLP
//
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