(data stored in ACNUC1104 zone)

SWISSPROT: D3VIK9_XENNA

ID   D3VIK9_XENNA            Unreviewed;       312 AA.
AC   D3VIK9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|RuleBase:RU004066, ECO:0000256|SAAS:SAAS00342015};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|RuleBase:RU004066, ECO:0000256|SAAS:SAAS00342002};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01516,
GN   ECO:0000313|EMBL:CBJ88559.1};
GN   OrderedLocusNames=XNC1_0485 {ECO:0000313|EMBL:CBJ88559.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88559.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88559.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate. {ECO:0000256|HAMAP-Rule:MF_01516,
CC       ECO:0000256|SAAS:SAAS00342020}.
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_01516,
CC         ECO:0000256|RuleBase:RU004066, ECO:0000256|SAAS:SAAS01117895};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01516,
CC       ECO:0000256|SAAS:SAAS00342012}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|SAAS:SAAS00538819}.
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DR   EMBL; FN667742; CBJ88559.1; -; Genomic_DNA.
DR   RefSeq; WP_010845224.1; NC_014228.1.
DR   STRING; 406817.XNC1_0485; -.
DR   EnsemblBacteria; CBJ88559; CBJ88559; XNC1_0485.
DR   KEGG; xne:XNC1_0485; -.
DR   eggNOG; ENOG4105C80; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000213792; -.
DR   KO; K00024; -.
DR   OMA; QCTPKVE; -.
DR   Proteomes; UP000008075; 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_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; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11540:SF22; PTHR11540:SF22; 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; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VIK9.
DR   SWISS-2DPAGE; D3VIK9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|RuleBase:RU000422,
KW   ECO:0000256|SAAS:SAAS00420673};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01516,
KW   ECO:0000256|RuleBase:RU004066, ECO:0000256|SAAS:SAAS00420680,
KW   ECO:0000313|EMBL:CBJ88559.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01516,
KW   ECO:0000256|RuleBase:RU000422, ECO:0000256|SAAS:SAAS00009822}.
FT   DOMAIN        1    145       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      147    308       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, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING      94     94       NAD. {ECO:0000256|HAMAP-Rule:MF_01516}.
FT   BINDING     119    119       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01516, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING     153    153       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01516, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING     227    227       NAD. {ECO:0000256|HAMAP-Rule:MF_01516}.
SQ   SEQUENCE   312 AA;  32682 MW;  7ACD98022628C35D CRC64;
     MKVAVLGAAG GIGQALALLL KTQLPSGSEL SLYDIAPVTP GVAVDLSHIP TEVKVTGFAG
     EDATPALAGA DVVLISAGVA RKPGMDRSDL FNINAGIIRN LVQQVAKTCP KALIGIITNP
     VNTTVAIAAE VLKKEGVYDK NRLFGVTTLD VIRSNTFVAE LKGKKLEDLE VPVIGGHSGV
     TILPLLSQIP DVSFTDEEIE ALTKRIQNAG TEVVEAKAGG GSATLSMGQA AARMGLSMIR
     GLQGESNVIE CSYVEGDGEH ARFFAQPVRL GKNGIEERLD IGKLSDFEQK ALDDMLGVLQ
     KDIELGEKCI NG
//

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