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Database: UniProt/TrEMBL
Entry: A0A127H136_9GAMM
LinkDB: A0A127H136_9GAMM
Original site: A0A127H136_9GAMM 
ID   A0A127H136_9GAMM        Unreviewed;       327 AA.
AC   A0A127H136;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   05-JUL-2017, entry version 11.
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   ORFNames=AK825_11665 {ECO:0000313|EMBL:AMN68270.1};
OS   Psychrobacter sp. P11G5.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=1699624 {ECO:0000313|EMBL:AMN68270.1};
RN   [1] {ECO:0000313|EMBL:AMN68270.1, ECO:0000313|Proteomes:UP000073122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P11G5 {ECO:0000313|EMBL:AMN68270.1,
RC   ECO:0000313|Proteomes:UP000073122};
RX   PubMed=26879123; DOI=10.1186/s12864-016-2445-4;
RA   Moghadam M.S., Albersmeier A., Winkler A., Cimmino L., Rise K.,
RA   Hohmann-Marriott M.F., Kalinowski J., Ruckert C., Wentzel A., Lale R.;
RT   "Isolation and genome sequencing of four Arctic marine Psychrobacter
RT   strains exhibiting multicopper oxidase activity.";
RL   BMC Genomics 17:117-117(2016).
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; CP012533; AMN68270.1; -; Genomic_DNA.
DR   RefSeq; WP_068037600.1; NZ_CP012533.1.
DR   EnsemblBacteria; AMN68270; AMN68270; AK825_11665.
DR   KEGG; psyg:AK825_11665; -.
DR   PATRIC; fig|1699624.3.peg.2416; -.
DR   KO; K00024; -.
DR   Proteomes; UP000073122; Chromosome.
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   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; IPR016040; NAD(P)-bd_dom.
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:UP000073122};
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:AMN68270.1};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN        6    152       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      156    323       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   327 AA;  35158 MW;  5ACD64E4C6587CAF CRC64;
     MKQPLRVAVT GAAGNISYAM LFRIASGEML GKDQPVILQL LEITPALDAL KGVVMELEDC
     AFPLLAGIVQ TDDANVAFKD IDYALLVGAR PRGPGMERKD LLEANAAIFS AQGKALNDVA
     SRDVKVLVVG NPANTNALIA QRNAPDLDPR NFTAMTRLDH NRAMAQLADK TDSTVNDIKN
     MTIWGNHSST QYPDLTACTV NGKPALDLVD RDWYENTYIP EVQQRGAAII KARGASSAAS
     AANAAIAHMR TWALGSDEND WVSMGVYSNG EYGIAEGLIY SFPVTCANGD WSIVDGVDVS
     SDFSKEKMAA TEQELSEERD AVAHLLP
//
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