ID E1QUL2_VULDI Unreviewed; 309 AA.
AC E1QUL2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382};
GN OrderedLocusNames=Vdis_1757 {ECO:0000313|EMBL:ADN51131.1};
OS Vulcanisaeta distributa (strain DSM 14429 / JCM 11212 / NBRC 100878 /
OS IC-017).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=572478 {ECO:0000313|EMBL:ADN51131.1, ECO:0000313|Proteomes:UP000006681};
RN [1] {ECO:0000313|EMBL:ADN51131.1, ECO:0000313|Proteomes:UP000006681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017
RC {ECO:0000313|Proteomes:UP000006681};
RX PubMed=21304741;
RA Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., Lucas S.,
RA Nolan M., Glavina Del Rio T., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S.,
RA Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Vulcanisaeta distributa type strain (IC-
RT 017).";
RL Stand. Genomic Sci. 3:117-125(2010).
RN [2] {ECO:0000313|Proteomes:UP000006681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017
RC {ECO:0000313|Proteomes:UP000006681};
RX DOI=10.4056/sigs.1113067;
RA Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., Lucas S.,
RA Nolan M., Glavina Del Rio T., Cheng J., Bruce D., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y., Jeffries C., Rohde M., Spring S., Goker M.,
RA Wirth R., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA Klenk H., Kyrpides N.;
RT "Complete genome sequence of Vulcanisaeta distributa type strain (IC-
RT 017T).";
RL Stand. Genomic Sci. 3:117-125(2010).
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC {ECO:0000256|ARBA:ARBA00008104, ECO:0000256|RuleBase:RU003369}.
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DR EMBL; CP002100; ADN51131.1; -; Genomic_DNA.
DR RefSeq; WP_013336856.1; NC_014537.1.
DR AlphaFoldDB; E1QUL2; -.
DR STRING; 572478.Vdis_1757; -.
DR GeneID; 9752700; -.
DR KEGG; vdi:Vdis_1757; -.
DR eggNOG; arCOG00246; Archaea.
DR HOGENOM; CLU_045401_2_1_2; -.
DR OMA; ASCAEYI; -.
DR OrthoDB; 2596at2157; -.
DR Proteomes; UP000006681; Chromosome.
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:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR CDD; cd01339; LDH-like_MDH; 1.
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; IPR011275; Malate_DH_type3.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW Reference proteome {ECO:0000313|Proteomes:UP000006681}.
FT DOMAIN 2..140
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 145..302
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 6..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 93
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 309 AA; 33930 MW; E25C0BBC61F1C688 CRC64;
MITIIGSGRV GATTAAFLMF FEPDNEIVLI DVIKNLPQGE ALDLNHAAAI LGKSVRYRGS
NDYKDMEGSD LVIVTAGLAR KPGMTREELA AKNAEIVASI AEQIRKYAPN SIVIITTNPL
DAMVYVLYKK LGFPRNRVIG FSGVLDSQRM AYYASLLVGI APESIIPVVL GQHGENMYPV
PEASFVYGKP LTEFITKEQY DDIVKKTVQA GAEITNLRGF SSNWGPAAGL ALMVDSIKKD
RKRIFEASVY LDGEYGVRDV FAEVPVVLGK NGVEKIIELN LNEEQKKKFL ASVEAIRKNL
MQVPPQFLS
//