ID K2KMI0_HELPX Unreviewed; 450 AA.
AC K2KMI0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
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 ECO:0000313|EMBL:EKE87767.1};
GN ORFNames=OUI_0086 {ECO:0000313|EMBL:EKE87767.1};
OS Helicobacter pylori R036d.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1145113 {ECO:0000313|EMBL:EKE87767.1, ECO:0000313|Proteomes:UP000006759};
RN [1] {ECO:0000313|EMBL:EKE87767.1, ECO:0000313|Proteomes:UP000006759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R036d {ECO:0000313|EMBL:EKE87767.1,
RC ECO:0000313|Proteomes:UP000006759};
RA Blanchard T.G., Czinn S.J., McCracken C.M., Abolude K.A., Shefchek K.S.,
RA Maroo A.M., Santana-Cruz I.S., Tallon L.J., Ficke F.W.F.;
RT "Comparative Sequence Analysis of H. pylori isolates.";
RL Submitted (AUG-2012) 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}.
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:EKE87767.1}.
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DR EMBL; AMOT01000001; EKE87767.1; -; Genomic_DNA.
DR RefSeq; WP_000061416.1; NZ_AMOT01000001.1.
DR AlphaFoldDB; K2KMI0; -.
DR PATRIC; fig|1145113.3.peg.86; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000006759; 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-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; 45A6E6E5362EB109 CRC64;
MSMEFDAVII GGGVSGCATF YTLSEYSSLK RVAIVEKCSK LAQISSSAKA NSQTIHDGSI
ETNYTPEKAK KVRLSAYKTR QYALNKGLQN EVIFETQKMA IGVGDEECEF MKKRYESFKE
IFVGLEEFDK QKIKELEPNV ILGANGIDRH ENIIGHGYQK DWSTMNFAKL SENFVEEALK
LKPNNQVFLN FKVKKIEKRN DTYAVISEDA EEVYAKFVLV NAGSYALPLA QSMGYGLDLG
CLPVAGSFYF VPDLLRGKVY TVQNPKLPFA AVHGDPDAVI KGKTRIGPTA LTMPKLERNK
CWLKGISLEL LKMDLNKDVF KIAFDLMSDK EIRNYVFKNM VFELPVIGKR KFLKDAQKII
PSLSLEDLEY AHGFGEVRPQ VLDRTKRKLE LGEKKICTHK GITFNMTPSP GATSCLQNAL
VDSQEIAAYL GESFELERFY KDLSPEELEN
//
