ID A0A0A2G739_9PORP Unreviewed; 333 AA.
AC A0A0A2G739;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Malate dehydrogenase {ECO:0000313|EMBL:KGN99066.1};
GN ORFNames=HQ36_00940 {ECO:0000313|EMBL:KGN99066.1};
OS Porphyromonas gingivicanis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=266762 {ECO:0000313|EMBL:KGN99066.1, ECO:0000313|Proteomes:UP000030134};
RN [1] {ECO:0000313|EMBL:KGN99066.1, ECO:0000313|Proteomes:UP000030134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-022 OH1391 {ECO:0000313|Proteomes:UP000030134};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas gingivicanis strain:COT-022_OH1391 Genome sequencing.";
RL Submitted (AUG-2014) 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:KGN99066.1}.
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DR EMBL; JQZW01000002; KGN99066.1; -; Genomic_DNA.
DR RefSeq; WP_025842699.1; NZ_JQZW01000002.1.
DR AlphaFoldDB; A0A0A2G739; -.
DR STRING; 266762.HQ36_00940; -.
DR eggNOG; COG0039; Bacteria.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000030134; 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:UP000030134}.
FT DOMAIN 8..145
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 150..284
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; 36407 MW; 43A866C6AD6B8D90 CRC64;
MNFLTEDKLT FVGAAGMIGS NMAQTAAMMR LTPNICLYDP FIQGLEGVAE EMRHCGFEGL
NLTFTDDIEK AFTGTKYIVS AGGAPRKEGM TREDLLRGNS EIAAELGRNI KRYCPDVHHV
TIIFNPADIT GLVTLVHSGL KPSQVTTLAA LDTTRLQSEL AKHFGVLQSK VTNCRTYGGH
GEMMAVFAST AQVEDTPLST LIGTDKLSNE EWIALKERVV KGGANIIKLR GRSSFQSPSY
VSVKMIAAAM GGEPFVQPSG CYVANEKYNH IMMAMENNIT KEGVICHEMK GTAEELALLD
QSYEHLCALR NQVIDMGILP PLTEWSKINP NLK
//