ID   B3C6Q0_9BACE            Unreviewed;       346 AA.
AC   B3C6Q0;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   SubName: Full=Lactate/malate dehydrogenase, NAD binding domain protein {ECO:0000313|EMBL:EDV07024.1};
GN   ORFNames=BACINT_00586 {ECO:0000313|EMBL:EDV07024.1};
OS   Bacteroides intestinalis DSM 17393.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=471870 {ECO:0000313|EMBL:EDV07024.1, ECO:0000313|Proteomes:UP000004596};
RN   [1] {ECO:0000313|EMBL:EDV07024.1, ECO:0000313|Proteomes:UP000004596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV07024.1,
RC   ECO:0000313|Proteomes:UP000004596};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Bacteroides intestinalis (DSM 17393).";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDV07024.1, ECO:0000313|Proteomes:UP000004596}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17393 {ECO:0000313|EMBL:EDV07024.1,
RC   ECO:0000313|Proteomes:UP000004596};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|ARBA:ARBA00009613}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDV07024.1}.
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DR   EMBL; ABJL02000006; EDV07024.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3C6Q0; -.
DR   STRING; 471870.BACINT_00586; -.
DR   eggNOG; COG0039; Bacteria.
DR   Proteomes; UP000004596; Unassembled WGS sequence.
DR   GO; GO:0016615; F:malate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006108; P:malate 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; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
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|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369}.
FT   DOMAIN          21..158
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          163..321
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         26..32
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         52
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         112
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         136..138
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   346 AA;  37897 MW;  2EE1CDD212BED8F2 CRC64;
     MREIIFTFKY IKVMEFLTNE KLTIVGAAGM IGSNMAQTAI MMHLTPNICL YDPYGPGLEG
     VAEEMFHCGF EGLNLTYTSD IKEALTDAKY IVSSGGAARK AGMTREDLLK GNAAIAEEFG
     KNVKAYCPDV KHVVVIFNPA DITGLITLLY SGLKPSQVTT LAALDSTRLR SELAKHFHIS
     PDKVENCRTY GGHGEQMAVY ASTAKVDGKP LLEIIGTPAL TAEQWAEIQS KVTKGGANII
     NLRGRSSFQS PAYVSIEMIA AAMGGKPFRW PAGTYVHSHG FDHIMMAMET EITKDGVHYK
     ELKGTPEEEA KLKESYAHLC KLRDEVIGMG VLPEIKDWKS INPNID
//