(data stored in ACNUC1104 zone)

SWISSPROT: D3UYX1_XENBS

ID   D3UYX1_XENBS            Unreviewed;       312 AA.
AC   D3UYX1;
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:CBJ79499.1};
GN   OrderedLocusNames=XBJ1_0349 {ECO:0000313|EMBL:CBJ79499.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79499.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79499.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79499.1,
RC   ECO:0000313|Proteomes:UP000002045};
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; FN667741; CBJ79499.1; -; Genomic_DNA.
DR   RefSeq; WP_012986959.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0349; -.
DR   EnsemblBacteria; CBJ79499; CBJ79499; XBJ1_0349.
DR   GeneID; 8829974; -.
DR   KEGG; xbo:XBJ1_0349; -.
DR   PATRIC; fig|406818.4.peg.320; -.
DR   eggNOG; ENOG4105C80; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000213792; -.
DR   KO; K00024; -.
DR   OMA; QCTPKVE; -.
DR   BioCyc; XBOV406818:XBJ1_RS01520-MONOMER; -.
DR   Proteomes; UP000002045; 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; D3UYX1.
DR   SWISS-2DPAGE; D3UYX1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
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:CBJ79499.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
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    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, 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;  32662 MW;  1C9611B74661881B CRC64;
     MKVAVLGAAG GIGQALALLL KTQLPSGSEL SLYDIAPVTP GVAADLSHIP TEVKVTGFAG
     EDATPALVGA DVVLISAGVA RKPGMDRSDL FNINAGIIRN LVQQVAKACP KALIGIITNP
     VNTTVAIAAE VLKKEGVYDR NRLFGITTLD IIRSNTFVAE LKGKNSEELE VPVIGGHSGV
     TILPLLSQIQ GVSFTDEEVE ALTKRIQNAG TEVVEAKAGG GSATLSMGQA AARLGLSLIR
     GLQGESNVIE CSYVEGDGKY ARFFAQPVRL GKNGIEERLD IGKLSDFEQK SLDSMLGVLK
     KDIELGEKFI NG
//

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