ID A0A268U8G2_9HELI Unreviewed; 449 AA.
AC A0A268U8G2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=malate dehydrogenase (quinone) {ECO:0000256|ARBA:ARBA00013026};
DE EC=1.1.5.4 {ECO:0000256|ARBA:ARBA00013026};
DE AltName: Full=MQO {ECO:0000256|ARBA:ARBA00031550};
DE AltName: Full=Malate dehydrogenase [quinone] {ECO:0000256|ARBA:ARBA00030660};
GN ORFNames=BKH42_06665 {ECO:0000313|EMBL:PAF53295.1};
OS Helicobacter sp. 13S00482-2.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1476200 {ECO:0000313|EMBL:PAF53295.1, ECO:0000313|Proteomes:UP000216174};
RN [1] {ECO:0000313|EMBL:PAF53295.1, ECO:0000313|Proteomes:UP000216174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13S00482-2 {ECO:0000313|EMBL:PAF53295.1,
RC ECO:0000313|Proteomes:UP000216174};
RX PubMed=28827684; DOI=10.1038/s41598-017-09091-7;
RA Gilbert M.J., Duim B., Timmerman A.J., Zomer A.L., Wagenaar J.A.;
RT "Whole genome-based phylogeny of reptile-associated Helicobacter indicates
RT independent niche adaptation followed by diversification in a
RT poikilothermic host.";
RL Sci. Rep. 7:8387-8387(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + a quinone = a quinol + oxaloacetate;
CC Xref=Rhea:RHEA:46012, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.1.5.4;
CC Evidence={ECO:0000256|ARBA:ARBA00001139};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC oxaloacetate from (S)-malate (quinone route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005012}.
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:PAF53295.1}.
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DR EMBL; MLAT01000013; PAF53295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268U8G2; -.
DR OrthoDB; 5337444at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000216174; Unassembled WGS sequence.
DR GO; GO:0052589; F:malate dehydrogenase (menaquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0008924; F:malate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006231; MQO.
DR PANTHER; PTHR43104; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43104:SF2; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF06039; Mqo; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 449 AA; 50543 MW; 043FCB95D9C84B01 CRC64;
MENEFDVVII GGGVSGCAAF YTLSEYSDIK KIAIVEKCPQ LAMVSSSAKA NSQTIHDGSI
ETNYTVQKAK KVKLSAYKVR RYALNRNLQN QIIFENQKMA IGVGDEECEF MRKRHQDFKE
VFPELESFDK GTIRKIEPKV ILQANGEDRP ENVIASGFKK DWCAMNFGLL AEDFVREGKR
IKPNNEVFLN YKVQKIQPHS GGYTIISDDS REIHAKFVLV DAGSYALPLA QSMGYGLELG
CLPVAGSFYF VPDLLRGKVY TVQNPKLPFA AVHGDPDVVI KGKTRLGPTA LAMPKLERNK
HLFGGISLDL LKMDLNREVF KITWDLLSDK EIRDYVVKNV IFELPYVGKK KFLKDARKII
PSLRLEDLSY ASGFGEVRPQ VLDRVNKKLE LGEKKISTNK GITFNMTPSP GATSCLQNAL
IDAREITDYL GARFDLERFY QDLSPEELD
//
