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Database: UniProt/TrEMBL
Entry: A0A1C9WA38_9GAMM
LinkDB: A0A1C9WA38_9GAMM
Original site: A0A1C9WA38_9GAMM 
ID   A0A1C9WA38_9GAMM        Unreviewed;       326 AA.
AC   A0A1C9WA38;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422, ECO:0000256|SAAS:SAAS00369716};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422, ECO:0000256|SAAS:SAAS00369716};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517,
GN   ECO:0000313|EMBL:AOS98019.1};
GN   ORFNames=AUP74_02622 {ECO:0000313|EMBL:AOS98019.1};
OS   Microbulbifer sp. CCB-MM1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Microbulbiferaceae; Microbulbifer.
OX   NCBI_TaxID=1769779 {ECO:0000313|EMBL:AOS98019.1, ECO:0000313|Proteomes:UP000095672};
RN   [1] {ECO:0000313|EMBL:AOS98019.1, ECO:0000313|Proteomes:UP000095672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCB-MM1 {ECO:0000313|EMBL:AOS98019.1,
RC   ECO:0000313|Proteomes:UP000095672};
RA   Moh T.H., Dinesh B., Lau N.-S., Go F., Alexander Chong S.-C.;
RT   "Complete genome sequence of Microbulbifer sp. CCB-MM1, a halophile
RT   isolated from Matang Mangrove Forest, Perak.";
RL   Submitted (JAN-2016) 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:RU000422,
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; CP014143; AOS98019.1; -; Genomic_DNA.
DR   RefSeq; WP_069947951.1; NZ_CP014143.1.
DR   EnsemblBacteria; AOS98019; AOS98019; AUP74_02622.
DR   KEGG; micc:AUP74_02622; -.
DR   PATRIC; fig|1769779.3.peg.2613; -.
DR   KO; K00024; -.
DR   Proteomes; UP000095672; 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   Gene3D; 3.90.110.10; -; 1.
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; IPR036291; NAD(P)-bd_dom_sf.
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:UP000095672};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369, ECO:0000313|EMBL:AOS98019.1};
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   326 AA;  35003 MW;  28137C608DCDDD6E CRC64;
     MKAPVRVAVT GAAGQISYSL LFRIASGEML GKDQPVILQL LEITPALEAL KGVAMELEDC
     AFPLLAGIVQ SDDANVAFKD ADYALLVGAR PRGPGMERKD LLEANAAIFS AQGKALNDVA
     SRNVKVLVVG NPANTNALIA QRNAPDLDPR NFTAMTRLDH NRALSQLAGK TSSSVNDITH
     MTIWGNHSST QYPDLHQVKV GGEAAMDKVE QDWYENDFIP TVQQRGAAII KARGASSAAS
     AANAAIDHMR DWALGTAEGD WTSMAVYSDG SYGIQEGLIY SFPCTCKDGD WTVVQGVDIN
     EFSREKMAAT EKELAEERDA VAHLLP
//
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