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
//