ID H8H6S2_HELPX Unreviewed; 450 AA.
AC H8H6S2;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Probable malate:quinone oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00212};
DE EC=1.1.5.4 {ECO:0000256|HAMAP-Rule:MF_00212};
DE AltName: Full=MQO {ECO:0000256|HAMAP-Rule:MF_00212};
DE AltName: Full=Malate dehydrogenase [quinone] {ECO:0000256|HAMAP-Rule:MF_00212};
GN Name=mqo {ECO:0000256|HAMAP-Rule:MF_00212};
GN ORFNames=HPELS_00445 {ECO:0000313|EMBL:AFF19673.1};
OS Helicobacter pylori ELS37.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1055527 {ECO:0000313|EMBL:AFF19673.1, ECO:0000313|Proteomes:UP000007885};
RN [1] {ECO:0000313|EMBL:AFF19673.1, ECO:0000313|Proteomes:UP000007885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ELS37 {ECO:0000313|EMBL:AFF19673.1,
RC ECO:0000313|Proteomes:UP000007885};
RA Bertoli M.T., Kersulyte D., Pascasio M.A., Berg D.E.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|HAMAP-
CC Rule:MF_00212};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_00212};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC oxaloacetate from (S)-malate (quinone route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005012, ECO:0000256|HAMAP-Rule:MF_00212}.
CC -!- SIMILARITY: Belongs to the MQO family. {ECO:0000256|HAMAP-
CC Rule:MF_00212}.
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DR EMBL; CP002953; AFF19673.1; -; Genomic_DNA.
DR RefSeq; WP_000061451.1; NC_017063.1.
DR AlphaFoldDB; H8H6S2; -.
DR KEGG; hpe:HPELS_00445; -.
DR PATRIC; fig|1055527.3.peg.86; -.
DR HOGENOM; CLU_613842_0_0_7; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000007885; Chromosome.
DR GO; GO:0052589; F:malate dehydrogenase (menaquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0008924; F:malate dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00212; MQO; 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 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00212};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00212};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00212}; Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
SQ SEQUENCE 450 AA; 50670 MW; F5A0CE4185874FA8 CRC64;
MSMEFDAVII GGGVSGCATF YTLSEYSSLK RVAIVEKCSK LAQISSSAKA NSQTIHDGSI
ETNYTPEKAK KVRLSAYKTR QYALNKGLQN EVIFETQKMA IGVGDEECEF MKKRYESFKE
IFVGLEEFDK QKIKELEPNV ILGANGIDRH ENIVGHGYQK DWSTMNFAKL SENFVEEALK
LKPNNQVFLN FKVKKIEKRN DTYAVISEDA EEVYAKFVLV NAGSYALPLA QSMGYGLDLG
CLPVAGSFYF VPDLLRGKVY TVQNPKLPFA AVHGDPDAVI KGKTRIGPTA LTMPKLERNK
CWLKGISLEL LKMDLNKDVF KIAFDLMSDK EIRNYVFKNM VFELPIIGKR KFLKDAQKII
PSLSLEDLEY AHGFGEVRPQ VLDRTKRKLE LGEKKICTHK GITFNMTPSP GATSCLQNAL
VDSQEIAAYL GESFELERFY KDLSPEELEN
//
