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Database: UniProt
Entry: F8QVS9_PECCA
LinkDB: F8QVS9_PECCA
Original site: F8QVS9_PECCA 
ID   F8QVS9_PECCA            Unreviewed;       146 AA.
AC   F8QVS9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|RuleBase:RU000422};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU000422};
DE   Flags: Fragment;
GN   Name=mdh {ECO:0000313|EMBL:ADN23193.1};
OS   Pectobacterium carotovorum (Erwinia carotovora).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=554 {ECO:0000313|EMBL:ADN23193.1};
RN   [1] {ECO:0000313|EMBL:ADN23193.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=102 {ECO:0000313|EMBL:ADN23200.1}, 109
RC   {ECO:0000313|EMBL:ADN23201.1}, 121 {ECO:0000313|EMBL:ADN23202.1}, 2
RC   {ECO:0000313|EMBL:ADN23195.1}, 3 {ECO:0000313|EMBL:ADN23196.1}, A10.1
RC   {ECO:0000313|EMBL:ADN23168.1}, A10.2 {ECO:0000313|EMBL:ADN23169.1},
RC   A16 {ECO:0000313|EMBL:ADN23170.1}, A18 {ECO:0000313|EMBL:ADN23172.1},
RC   A6.2 {ECO:0000313|EMBL:ADN23167.1}, C140.2
RC   {ECO:0000313|EMBL:ADN23177.1}, C144 {ECO:0000313|EMBL:ADN23182.1}, C3
RC   {ECO:0000313|EMBL:ADN23174.1}, C338 {ECO:0000313|EMBL:ADN23187.1},
RC   C380 {ECO:0000313|EMBL:ADN23189.1}, M30 {ECO:0000313|EMBL:ADN23192.1},
RC   and N78 {ECO:0000313|EMBL:ADN23193.1};
RA   Nabhan S.A., Debener T., Linde M., Wydra K.D.;
RT   "Fingerprinting methods (AFLP, MLST) for identification and
RT   characterization of pectolytic, soft rot causing bacterial strains from
RT   Syria in comparison to strains from worldwide origin.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000256|ARBA:ARBA00003966}.
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; EC=1.1.1.37;
CC         Evidence={ECO:0000256|RuleBase:RU000422};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008824}.
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DR   EMBL; HM156942; ADN23167.1; -; Genomic_DNA.
DR   EMBL; HM156943; ADN23168.1; -; Genomic_DNA.
DR   EMBL; HM156944; ADN23169.1; -; Genomic_DNA.
DR   EMBL; HM156945; ADN23170.1; -; Genomic_DNA.
DR   EMBL; HM156947; ADN23172.1; -; Genomic_DNA.
DR   EMBL; HM156949; ADN23174.1; -; Genomic_DNA.
DR   EMBL; HM156952; ADN23177.1; -; Genomic_DNA.
DR   EMBL; HM156957; ADN23182.1; -; Genomic_DNA.
DR   EMBL; HM156962; ADN23187.1; -; Genomic_DNA.
DR   EMBL; HM156964; ADN23189.1; -; Genomic_DNA.
DR   EMBL; HM156967; ADN23192.1; -; Genomic_DNA.
DR   EMBL; HM156968; ADN23193.1; -; Genomic_DNA.
DR   EMBL; HM156970; ADN23195.1; -; Genomic_DNA.
DR   EMBL; HM156971; ADN23196.1; -; Genomic_DNA.
DR   EMBL; HM156975; ADN23200.1; -; Genomic_DNA.
DR   EMBL; HM156976; ADN23201.1; -; Genomic_DNA.
DR   EMBL; HM156977; ADN23202.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8QVS9; -.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|RuleBase:RU000422};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN          1..101
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          103..145
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADN23193.1"
FT   NON_TER         146
FT                   /evidence="ECO:0000313|EMBL:ADN23193.1"
SQ   SEQUENCE   146 AA;  15237 MW;  2208BF1DF0C8F01C CRC64;
     DLSHIPTAVK IKGYSGEDAK PALAGADIVL ISAGVARKPG MDRSDLFNVN AGIVRNLVEQ
     IAVTCPKACI GIITNPVNTT VAIAAEVLKK AGVYDKNKLF GVTTLDIIRS NTFVAELKGK
     QPQDINVPVI GGHSGVTILP LLSQVP
//
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