ID D3UHK6_HELM1 Unreviewed; 449 AA.
AC D3UHK6;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
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 OrderedLocusNames=HMU07210 {ECO:0000313|EMBL:CBG39978.1};
OS Helicobacter mustelae (strain ATCC 43772 / LMG 18044 / NCTC 12198 / 12198)
OS (Campylobacter mustelae).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=679897 {ECO:0000313|EMBL:CBG39978.1, ECO:0000313|Proteomes:UP000001522};
RN [1] {ECO:0000313|EMBL:CBG39978.1, ECO:0000313|Proteomes:UP000001522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43772 / LMG 18044 / NCTC 12198 / 12198
RC {ECO:0000313|Proteomes:UP000001522};
RX PubMed=20219135; DOI=10.1186/1471-2164-11-164;
RA O'Toole P.W., Snelling W.J., Canchaya C., Forde B.M., Hardie K.R.,
RA Josenhans C., Graham R.L.J., McMullan G., Parkhill J., Belda E.,
RA Bentley S.D.;
RT "Comparative genomics and proteomics of Helicobacter mustelae, an
RT ulcerogenic and carcinogenic gastric pathogen.";
RL BMC Genomics 11:164-164(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN555004; CBG39978.1; -; Genomic_DNA.
DR RefSeq; WP_013023056.1; NC_013949.1.
DR AlphaFoldDB; D3UHK6; -.
DR STRING; 679897.HMU07210; -.
DR KEGG; hms:HMU07210; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_613842_0_0_7; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000001522; Chromosome.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001522}.
SQ SEQUENCE 449 AA; 50905 MW; DCDD2603ECD45B6A CRC64;
MREFDVVIIG GGVSGCAAFY VLSEYTNVKS IAIVDKCDKW ANISSSSKAN SQTIHDGSIE
TNYTAEKAKK VRLSALKVRN YALQKNLQNK VIFEDQKMAI GIGDKECDVM KQRYEDFLDV
FPDMQFFDKQ KIKLLEPKVI EGYDGRDRFE DVVGMGYEKA WCAMNFGLLS EHFIEEGMNK
GKENQTFLNF WVKKIEPRGD GYAVISKENE EIYAKFVLVD AGSYALPLAQ SMGYGMDLGC
LPVAGSFYFV PDLLRGKVYT VQNPKLPFAA LHGDPDVVIK GKTRIGPTAL AMPKLERGKH
WYSKLSLELL KLDLNMDVMK IAADLLMDKE IRDYVIKNMI FEMPYIGKRK FLKDARKIIP
SLRLSDLHYA EGFGEVRPQV LDRKARKLVL GEKKIATQRG ITFNMTPSPG ATSCLQNAMI
DAEEIVQYLQ CNFEKERFLK ELCPEELDA
//