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Database: UniProt/TrEMBL
Entry: A0A0S2KCM3_9GAMM
LinkDB: A0A0S2KCM3_9GAMM
Original site: A0A0S2KCM3_9GAMM 
ID   A0A0S2KCM3_9GAMM        Unreviewed;       326 AA.
AC   A0A0S2KCM3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   05-JUL-2017, entry version 13.
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=PS2015_1201 {ECO:0000313|EMBL:ALO45860.1};
OS   Pseudohongiella spirulinae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudohongiella.
OX   NCBI_TaxID=1249552 {ECO:0000313|EMBL:ALO45860.1, ECO:0000313|Proteomes:UP000065641};
RN   [1] {ECO:0000313|EMBL:ALO45860.1, ECO:0000313|Proteomes:UP000065641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 32221 {ECO:0000313|EMBL:ALO45860.1,
RC   ECO:0000313|Proteomes:UP000065641};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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; CP013189; ALO45860.1; -; Genomic_DNA.
DR   RefSeq; WP_058021359.1; NZ_CP013189.1.
DR   EnsemblBacteria; ALO45860; ALO45860; PS2015_1201.
DR   KEGG; pspi:PS2015_1201; -.
DR   PATRIC; fig|1249552.3.peg.1206; -.
DR   KO; K00024; -.
DR   Proteomes; UP000065641; 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:UP000065641};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000065641};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN        6    146       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      157    319       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND      12     18       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   NP_BIND     130    132       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    188    188       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                1}.
FT   BINDING      93     93       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING      99     99       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     106    106       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     113    113       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     132    132       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     163    163       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
SQ   SEQUENCE   326 AA;  35067 MW;  89CA86CF70DD8BF8 CRC64;
     MAKAPVRVAV TGAAGQISYS LLFRIAAGEM LGKDQPVILQ LLEITPALEA LKGVVMELED
     CAFPLVQGFV QTDDPNVAFK DADYCLLVGA RPRGPGMERK DLLEANAAIF SVQGKAINDN
     ASRDVKVLVV GNPANTNALI AYRNAPDLKP GQFTAMTRLD HNRAIAQLAE KTGQHSTDVD
     GMIIWGNHSA TQYPDVHHTT VDGRKALDLV DMDWLTSTFI PNVQQRGAAI IKARGLSSAA
     SAANAAIEHM RDWALGTNGK IVSMGIHSDG SYGIAEGLIY SFPVTCENGQ YSIVQGLDIN
     DFSRDLMSKT EKELEEERAG VAHLLP
//
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