ID A0A1C7H2G0_9BACE Unreviewed; 333 AA.
AC A0A1C7H2G0;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:ANU58815.1};
GN ORFNames=A4V03_15615 {ECO:0000313|EMBL:ANU58815.1}, FMM78_15260
GN {ECO:0000313|EMBL:NDO60991.1};
OS Bacteroides caecimuris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1796613 {ECO:0000313|EMBL:ANU58815.1, ECO:0000313|Proteomes:UP000092631};
RN [1] {ECO:0000313|Proteomes:UP000092631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I48 {ECO:0000313|Proteomes:UP000092631};
RA Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA McCoy K.D., Macpherson A.J.;
RT "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT Diverse Mouse Microbiota 2 (sDMDMm2).";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANU58815.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I48 {ECO:0000313|EMBL:ANU58815.1};
RA Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA McCoy K.D., Macpherson A.J.;
RT "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT Diverse Mouse Microbiota 2 (sDMDMm2).";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:NDO60991.1, ECO:0000313|Proteomes:UP000589339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD237 {ECO:0000313|EMBL:NDO60991.1,
RC ECO:0000313|Proteomes:UP000589339};
RA Elie C., Mathieu A., Saliou A., Darnaud M., Leulier F., Tamellini A.;
RT "Draft genome sequences of 15 bacterial species constituting the stable
RT defined intestinal microbiota of the GM15 gnotobiotic mouse model.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000256|ARBA:ARBA00009613}.
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DR EMBL; CP015401; ANU58815.1; -; Genomic_DNA.
DR EMBL; VIRD01000060; NDO60991.1; -; Genomic_DNA.
DR RefSeq; WP_065539603.1; NZ_VIRD01000060.1.
DR AlphaFoldDB; A0A1C7H2G0; -.
DR STRING; 1796613.A4V03_15615; -.
DR GeneID; 82188570; -.
DR KEGG; bcae:A4V03_15615; -.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000092631; Chromosome.
DR Proteomes; UP000589339; 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:UP000092631}.
FT DOMAIN 8..145
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 150..311
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 180
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 86
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 99
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 123..125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 333 AA; 36432 MW; 030B7A45C320357F CRC64;
MEFLTNEKLT IVGAAGMIGS NMAQTAMMMK LTPNICLYDP FAPALEGVAE ELYHCGFEGV
NLTYTSDIKE ALTGASYIVS SGGAARKAGM TREDLLKGNA EIAAQFGKDV RQYCPNVKHI
VVIFNPADIT GLITLLYAGL KPSQVSTLAA LDSTRLQNEL VKYFHIPASD IQNCRTYGGH
GEQMAVFAST TKIKGEPLTD FIGTTRLPLT EWEALKVRVI QGGKHIIDLR GRSSFQSPAY
LSIEMIAAAM GGQPFRWPAG AYVSNGKFDH IMMAMETSIT KDGVTYKEIA GTPAEQEELE
KSYEHLCKLR DEVIEMGIIP AIKDWHTLNP NIK
//
