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Database: UniProt
Entry: A0A0A2MPC6_9FLAO
LinkDB: A0A0A2MPC6_9FLAO
Original site: A0A0A2MPC6_9FLAO 
ID   A0A0A2MPC6_9FLAO        Unreviewed;       504 AA.
AC   A0A0A2MPC6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=Q764_03340 {ECO:0000313|EMBL:KGO90115.1};
OS   Flavobacterium suncheonense GH29-5 = DSM 17707.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1121899 {ECO:0000313|EMBL:KGO90115.1, ECO:0000313|Proteomes:UP000030121};
RN   [1] {ECO:0000313|EMBL:KGO90115.1, ECO:0000313|Proteomes:UP000030121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GH29-5 {ECO:0000313|EMBL:KGO90115.1,
RC   ECO:0000313|Proteomes:UP000030121};
RA   Zeng Z., Chen C.;
RL   Submitted (SEP-2013) 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:KGO90115.1}.
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DR   EMBL; JRLW01000003; KGO90115.1; -; Genomic_DNA.
DR   RefSeq; WP_026981098.1; NZ_KE387020.1.
DR   AlphaFoldDB; A0A0A2MPC6; -.
DR   STRING; 1121899.GCA_000430025_00052; -.
DR   eggNOG; COG0579; Bacteria.
DR   OrthoDB; 9763983at2; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000030121; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00212}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   504 AA;  55900 MW;  1E4D0644D3F5702D CRC64;
     MTTKTTTQKS EADVVLIGAG IMSATLGLLL KELQPNLKIE IFERLDVAAA ESSDAWNNAG
     TGHAAFCELN YTPEKPDGSI DTTKAVKIVE AFEVSRQFWA YLVEKGLLKN PESFIKHVPH
     MSFVWGEKNT KYLKKRYDAL QQFHLFKEME YSEDPQTIKE WAPLIMEGRK GAKKVAATTM
     KYGTDVNFGA LTRSIFKYLE TLDGVTLHFN HEVKKLRRYD DGTWRVRVKD LETGGKKRVK
     TKFVFIGAGG GSLLLLEKAG IPEGEGYGGF PVSGQWLKCT NEELIAKHQV KVYGKAAVGA
     PPMSVPHIDT RMIDGKKALL FGPYAGFSTK FLKNGSYLDL AKSIQLDNIK PMLSAGINNI
     PLTKYLIEQV FQSSEDRMKA LREYLPDAKP EDWTLENAGQ RVQVIKKDKN GKGVLEFGTE
     VVNCADGSLA VLLGASPGAS TAVSIMLDLL SRCFKDELAT PEWQAKLKEM IPSYGQSLNA
     NPQLADEIRY RTGTVLKLRD VATV
//
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