ID D8J4I4_HALJB Unreviewed; 304 AA.
AC D8J4I4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995};
DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995};
GN OrderedLocusNames=HacjB3_00765 {ECO:0000313|EMBL:ADJ13546.1};
GN ORFNames=C497_18567 {ECO:0000313|EMBL:ELY32979.1};
OS Halalkalicoccus jeotgali (strain DSM 18796 / CECT 7217 / JCM 14584 / KCTC
OS 4019 / B3).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halalkalicoccus.
OX NCBI_TaxID=795797 {ECO:0000313|EMBL:ADJ13546.1, ECO:0000313|Proteomes:UP000000390};
RN [1] {ECO:0000313|EMBL:ADJ13546.1, ECO:0000313|Proteomes:UP000000390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3 {ECO:0000313|EMBL:ADJ13546.1}, and DSM 18796 / CECT 7217 /
RC JCM 14584 / KCTC 4019 / B3 {ECO:0000313|Proteomes:UP000000390};
RX PubMed=20601480; DOI=10.1128/JB.00663-10;
RA Roh S.W., Nam Y.D., Nam S.H., Choi S.H., Park H.S., Bae J.W.;
RT "Complete genome sequence of Halalkalicoccus jeotgali B3(T), an extremely
RT halophilic archaeon.";
RL J. Bacteriol. 192:4528-4529(2010).
RN [2] {ECO:0000313|Proteomes:UP000011645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3 {ECO:0000313|Proteomes:UP000011645};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ELY32979.1, ECO:0000313|Proteomes:UP000011645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B3 {ECO:0000313|EMBL:ELY32979.1,
RC ECO:0000313|Proteomes:UP000011645};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000256|ARBA:ARBA00003966}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC Evidence={ECO:0000256|ARBA:ARBA00000774};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC {ECO:0000256|ARBA:ARBA00008104, ECO:0000256|RuleBase:RU003369}.
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DR EMBL; CP002062; ADJ13546.1; -; Genomic_DNA.
DR EMBL; AOHV01000045; ELY32979.1; -; Genomic_DNA.
DR RefSeq; WP_008418963.1; NZ_AXZD01000013.1.
DR AlphaFoldDB; D8J4I4; -.
DR STRING; 795797.HacjB3_00765; -.
DR GeneID; 9417947; -.
DR KEGG; hje:HacjB3_00765; -.
DR PATRIC; fig|795797.18.peg.157; -.
DR eggNOG; arCOG00246; Archaea.
DR HOGENOM; CLU_045401_1_1_2; -.
DR OMA; CYIIVLT; -.
DR OrthoDB; 2596at2157; -.
DR Proteomes; UP000000390; Chromosome.
DR Proteomes; UP000011645; Unassembled WGS sequence.
DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:InterPro.
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; IPR018177; L-lactate_DH_AS.
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 NCBIfam; NF041314; Malate_DH_Halo; 1.
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.
DR PROSITE; PS00064; L_LDH; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003369}.
FT DOMAIN 2..143
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 147..302
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 8..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 304 AA; 32557 MW; CC747A87B1F9D64D CRC64;
MTKVSVVGAA GTVGAAAAYN IALREIADEL VLVDIPEKED DTVGQAADVN HGVAYDANTT
VRQGGYEATE GSDVVVITAG IPRSPGQSRL DLAGDNAPIM ADIGSSIEEH NDDYVTITTS
NPVDLLNRHL YETGERAREK VIGFGGRLDS ARFRYVLAER FDTQVQNVEA TILGEHGDSQ
VPVFSKVRVD GRDPEFSDAE KEEILDELQE SAMNVIERKG ATEWGPATGV GHMVEAVIRD
TGEVFPASVP LSGEFGHSGV GLGVPAKLGS EGVEEVVEWD LDEYEREQLG AAADKLAEQY
DQID
//