GenomeNet

Database: UniProt
Entry: S4XEJ1_9CORY
LinkDB: S4XEJ1_9CORY
Original site: S4XEJ1_9CORY 
ID   S4XEJ1_9CORY            Unreviewed;       492 AA.
AC   S4XEJ1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
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=A606_06635 {ECO:0000313|EMBL:AGP30974.1};
OS   Corynebacterium terpenotabidum Y-11.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1200352 {ECO:0000313|EMBL:AGP30974.1, ECO:0000313|Proteomes:UP000014809};
RN   [1] {ECO:0000313|EMBL:AGP30974.1, ECO:0000313|Proteomes:UP000014809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y-11 {ECO:0000313|EMBL:AGP30974.1,
RC   ECO:0000313|Proteomes:UP000014809};
RA   Ruckert C., Albersmeier A., Al-Dilaimi A., Szczepanowski R., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium terpenotabidum Y-11 (=DSM
RT   44721).";
RL   Submitted (JUN-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   ---------------------------------------------------------------------------
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; CP003696; AGP30974.1; -; Genomic_DNA.
DR   AlphaFoldDB; S4XEJ1; -.
DR   STRING; 1200352.A606_06635; -.
DR   KEGG; cter:A606_06635; -.
DR   PATRIC; fig|1200352.3.peg.1352; -.
DR   eggNOG; COG0579; Bacteria.
DR   HOGENOM; CLU_028151_0_0_11; -.
DR   OrthoDB; 9763983at2; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000014809; 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   NCBIfam; TIGR01320; mal_quin_oxido; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000014809};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
SQ   SEQUENCE   492 AA;  53584 MW;  2A1B2A474957D4B2 CRC64;
     MSPAKNDHVD VALVGAGVIS TTLSVMLREL QPDWTQLIIE RQDIPASESS DPWNNAGTGH
     SALCELNYTP EVNGKIDTTK AVNINEKFQV SRQFWSYLVE NGTLGDPSEW INATPHMSFG
     HGEKQSAYIK ARYEALKDNP LFPDMHLTTD PEEFTAKVPL MGKGRDFSEQ VALSWIDAGT
     DINYGALTRQ YLDAVTAQGV EVRYGSQVTN VTREGSGWKL TVKNLHNGDT TTVHAKFVFI
     GAGGMALPLL QKAGIPEIKG FAGFPVSGQW LRCTNQELVD QHAAKVYGQA AVGAPPMSVP
     HLDTRVIDGK KGLLFGPYAG WTPKFLKQGS NLDLFKSLRP GNIPSYLGVA VKELGLTKYL
     VTEVLKNQAA RVESLREYMP DARDEDWELV TAGQRVQVIK PAKAPTFGTL EFGTALINSA
     DGSIAGLMGA SPGASIAPSA MLEVLQACFS DRIDAWTPKL KDMIPSFGGK LSEDLALYNQ
     QWDRSQKSLK LA
//
DBGET integrated database retrieval system