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Database: UniProt
Entry: A7I2F1_CAMHC
LinkDB: A7I2F1_CAMHC
Original site: A7I2F1_CAMHC 
ID   A7I2F1_CAMHC            Unreviewed;       297 AA.
AC   A7I2F1;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:ABS52307.1};
DE            EC=1.1.1.37 {ECO:0000313|EMBL:ABS52307.1};
GN   OrderedLocusNames=CHAB381_1136 {ECO:0000313|EMBL:ABS52307.1};
OS   Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 /
OS   CH001A).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360107 {ECO:0000313|EMBL:ABS52307.1, ECO:0000313|Proteomes:UP000002407};
RN   [1] {ECO:0000313|Proteomes:UP000002407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A
RC   {ECO:0000313|Proteomes:UP000002407};
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Nelson K.E.;
RT   "Complete genome sequence of Campylobacter hominis ATCC BAA-381, a
RT   commensal isolated from the human gastrointestinal tract.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|RuleBase:RU003369}.
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DR   EMBL; CP000776; ABS52307.1; -; Genomic_DNA.
DR   RefSeq; WP_012108991.1; NC_009714.1.
DR   AlphaFoldDB; A7I2F1; -.
DR   STRING; 360107.CHAB381_1136; -.
DR   KEGG; cha:CHAB381_1136; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_2_1_7; -.
DR   OMA; ASCAEYI; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000002407; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369,
KW   ECO:0000313|EMBL:ABS52307.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002407}.
FT   DOMAIN          1..141
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          146..287
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         7..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         118..120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   297 AA;  32238 MW;  D7C19F92A31C457C CRC64;
     MKISIIGAGN IGSNIVSQLL CKDFEISQIA LIDIFGDLAK ARALDLSHLA SVYNKKTEIS
     GSSDETLLKN SDIVVITAGK TRQAGQSRAD LLNDNAKIIS SCAKNVAKYA PEAIIILITN
     PVDTLAFVAY KASGFKKEKI IAMAGELDSA RLRYEIAKSE NVNVTDIKAS VVGAHNDEMQ
     ILEDEIYKFG KKFKPQNLSL IKENTINSGS KITALQKTSS FFAPAACSVK MIDAIINDKN
     EILICSVLDE NEIPIGRFVR LNKNGVAEIL PFDYGEKTKS GLENIKGQIL NLNKGKV
//
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