ID D1VXA5_9BACT Unreviewed; 330 AA.
AC D1VXA5;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=Lactate/malate dehydrogenase, NAD binding domain protein {ECO:0000313|EMBL:EFA98255.1};
GN ORFNames=HMPREF9019_0589 {ECO:0000313|EMBL:EFA98255.1};
OS Hoylesella timonensis CRIS 5C-B1.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=679189 {ECO:0000313|EMBL:EFA98255.1, ECO:0000313|Proteomes:UP000004001};
RN [1] {ECO:0000313|EMBL:EFA98255.1, ECO:0000313|Proteomes:UP000004001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIS 5C-B1 {ECO:0000313|EMBL:EFA98255.1,
RC ECO:0000313|Proteomes:UP000004001};
RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA Nelson K.E.;
RT "Genome Sequence of Prevotella timonensis CRIS 5C-B1.";
RL Submitted (DEC-2009) 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:EFA98255.1}.
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DR EMBL; ADEF01000010; EFA98255.1; -; Genomic_DNA.
DR RefSeq; WP_008122447.1; NZ_ADEF01000010.1.
DR AlphaFoldDB; D1VXA5; -.
DR eggNOG; COG0039; Bacteria.
DR Proteomes; UP000004001; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004001}.
FT DOMAIN 8..143
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 148..306
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 13..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 121..123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 330 AA; 35897 MW; 1855204941097275 CRC64;
MAFLTNEKLT IVGAAGMIGS NMVQTALSMG LTNNICLYDV FSPEGVAEEM RQSGFDAVNI
VATTDVKEAF TDAKYIISSG GAPRKAGMTR EDLLKGNCEI AEGLGKDIKK YCPDVKHVVI
IFNPADLTGL VTLLYSGLKP SQVTTLAALD STRLQSALAK KFNVMQTEVK GAATYGGHGE
QMAVFGSHVT ISGKPLTEII GTPEFSNEEW EQMKKDVTKG GAKIIELRGR SSFQSPAYLS
VEMIRSVMGG EPFRFPVGTY VSTDKYNHIM MAMKTTLDKT GAHYEVPQGT SEENAKLDAS
YEHLCKMRDE LVTLNIVPEI SEWSKINPNL
//