(data stored in ACNUC7421 zone)

SWISSPROT: A4AWN8_MARSH

ID   A4AWN8_MARSH            Unreviewed;       308 AA.
AC   A4AWN8;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00487};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_00487};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_00487};
GN   OrderedLocusNames=FB2170_01791 {ECO:0000313|EMBL:EAQ99652.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAQ99652.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAQ99652.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate. {ECO:0000256|HAMAP-Rule:MF_00487,
CC       ECO:0000256|SAAS:SAAS01087531}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.37; Evidence={ECO:0000256|HAMAP-Rule:MF_00487};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00487}.
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DR   EMBL; CP002157; EAQ99652.1; -; Genomic_DNA.
DR   RefSeq; WP_013305051.1; NC_014472.1.
DR   STRING; 313603.FB2170_01791; -.
DR   EnsemblBacteria; EAQ99652; EAQ99652; FB2170_01791.
DR   KEGG; fbc:FB2170_01791; -.
DR   eggNOG; ENOG4105C80; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000213794; -.
DR   KO; K00024; -.
DR   OMA; MDLMQTA; -.
DR   OrthoDB; 870724at2; -.
DR   BioCyc; MSP313603:G1GNS-619-MONOMER; -.
DR   Proteomes; UP000001602; 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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd01339; LDH-like_MDH; 1.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_00487; Malate_dehydrog_3; 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; IPR011275; Malate_DH_type3.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4AWN8.
DR   SWISS-2DPAGE; A4AWN8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00487, ECO:0000256|SAAS:SAAS01087535};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00487,
KW   ECO:0000256|RuleBase:RU003369, ECO:0000256|SAAS:SAAS01087526};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00487,
KW   ECO:0000256|SAAS:SAAS01087533}.
FT   DOMAIN        1    142       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      147    301       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND       7     12       NAD. {ECO:0000256|HAMAP-Rule:MF_00487}.
FT   NP_BIND     118    120       NAD. {ECO:0000256|HAMAP-Rule:MF_00487}.
FT   ACT_SITE    175    175       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00487, ECO:0000256|PIRSR:PIRSR000102-
FT                                1}.
FT   BINDING      32     32       NAD. {ECO:0000256|HAMAP-Rule:MF_00487}.
FT   BINDING      82     82       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00487}.
FT   BINDING      88     88       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00487, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING      95     95       NAD. {ECO:0000256|HAMAP-Rule:MF_00487}.
FT   BINDING     120    120       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00487, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING     151    151       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00487, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
SQ   SEQUENCE   308 AA;  32285 MW;  A90192EC534698D1 CRC64;
     MKVTVVGAGA VGASCAEYIA IKDFASEVVV LDIKEGYAEG KAMDLMQTAS LNGFDTKITG
     TTNDYSKTAG SDIAVITSGI PRKPGMTREE LIGINAGIVK TVSANLIEHS PNVILIVVSN
     PMDTMTYLVH KTTGLPKNKI IGMGGALDSA RFKYRLAEAM EAPISDIDGM VIGGHSDTGM
     VPLASHATRN SINVSEYLSE DRLNQVVEDT KVGGATLTKL LGTSAWYAPG AAVSSLVQAI
     ACDQKKMFPC STLLEGEYGL NDICIGVPVI LGKNGIEKVV DVPLSDAEKT KMQESAAGVT
     KTNGLLEV
//

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