ID   A0A177Y1N1_9VIBR        Unreviewed;       310 AA.
AC   A0A177Y1N1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   12-APR-2017, entry version 7.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|RuleBase:RU000422, ECO:0000256|SAAS:SAAS00671810};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|RuleBase:RU000422, ECO:0000256|SAAS:SAAS00671813};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01516};
GN   ORFNames=APB76_10005 {ECO:0000313|EMBL:OAJ94395.1};
OS   Vibrio bivalvicida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=1276888 {ECO:0000313|EMBL:OAJ94395.1, ECO:0000313|Proteomes:UP000078406};
RN   [1] {ECO:0000313|EMBL:OAJ94395.1, ECO:0000313|Proteomes:UP000078406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=605 {ECO:0000313|EMBL:OAJ94395.1,
RC   ECO:0000313|Proteomes:UP000078406};
RX   PubMed=26654527; DOI=10.1016/j.syapm.2015.10.006;
RA   Dubert J., Romalde J.L., Prado S., Barja J.L.;
RT   "Vibrio bivalvicida sp. nov., a novel larval pathogen for bivalve
RT   molluscs reared in a hatchery.";
RL   Syst. Appl. Microbiol. 39:8-13(2016).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate. {ECO:0000256|HAMAP-Rule:MF_01516,
CC       ECO:0000256|SAAS:SAAS00671814}.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC       {ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|RuleBase:RU000422,
CC       ECO:0000256|SAAS:SAAS00671812}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01516,
CC       ECO:0000256|SAAS:SAAS00671815}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|SAAS:SAAS00671811}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OAJ94395.1}.
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DR   EMBL; LLEI02000026; OAJ94395.1; -; Genomic_DNA.
DR   RefSeq; WP_049844370.1; NZ_LLEI02000026.1.
DR   Proteomes; UP000078406; Unassembled WGS sequence.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
DR   Gene3D; 3.40.50.720; -; 1.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_01516; Malate_dehydrog_1; 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; IPR010097; Malate_DH_type1.
DR   InterPro; IPR023958; Malate_DH_type1_bac.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000078406};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|RuleBase:RU000422,
KW   ECO:0000256|SAAS:SAAS00671817};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01516,
KW   ECO:0000256|RuleBase:RU003369, ECO:0000256|SAAS:SAAS00671818};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01516,
KW   ECO:0000256|RuleBase:RU000422, ECO:0000256|SAAS:SAAS00671816}.
FT   DOMAIN        1    145       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      147    309       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND       7     13       NAD. {ECO:0000256|HAMAP-Rule:MF_01516}.
FT   NP_BIND     117    119       NAD. {ECO:0000256|HAMAP-Rule:MF_01516}.
FT   ACT_SITE    177    177       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01516, ECO:0000256|PIRSR:PIRSR000102-
FT                                1}.
FT   BINDING      34     34       NAD. {ECO:0000256|HAMAP-Rule:MF_01516}.
FT   BINDING      81     81       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01516}.
FT   BINDING      87     87       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01516}.
FT   BINDING      94     94       NAD. {ECO:0000256|HAMAP-Rule:MF_01516}.
FT   BINDING     119    119       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01516}.
FT   BINDING     153    153       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01516}.
FT   BINDING     227    227       NAD. {ECO:0000256|HAMAP-Rule:MF_01516}.
SQ   SEQUENCE   310 AA;  32158 MW;  A225EECD194B1EEB CRC64;
     MKVAVIGAAG GIGQALALLL KNRLPAGSDL ALYDIAPVTP GVAADLSHIP TPVSIKGYAG
     EDPTPALEGA DVVLISAGVA RKPGMDRADL FNVNAGIVKS LAQRIADVCP KALVGIITNP
     VNTTVPIAAE VLKQAGVYDK RRLFGVTTLD VIRSETFVAD LKDKDPGDVR VPVIGGHSGV
     TILPLLSQVE GVEFSDEEVA ALTKRIQNAG TEVVEAKAGG GSATLSMGQA ACRFGLALVK
     ALQGEEVIEY AYVEGDGEHA PFFAQPVKLG KEGVEEVLSY GELSDFEKSA LDGMLETLNG
     DIQTGVDFVK
//