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Database: UniProt
Entry: A0A1D8P4T8_9FLAO
LinkDB: A0A1D8P4T8_9FLAO
Original site: A0A1D8P4T8_9FLAO 
ID   A0A1D8P4T8_9FLAO        Unreviewed;       494 AA.
AC   A0A1D8P4T8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=LPB138_02335 {ECO:0000313|EMBL:AOW19585.1};
OS   Urechidicola croceus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Urechidicola.
OX   NCBI_TaxID=1850246 {ECO:0000313|EMBL:AOW19585.1, ECO:0000313|Proteomes:UP000176050};
RN   [1] {ECO:0000313|EMBL:AOW19585.1, ECO:0000313|Proteomes:UP000176050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0138 {ECO:0000313|EMBL:AOW19585.1,
RC   ECO:0000313|Proteomes:UP000176050};
RA   Kim E., Yi H.;
RT   "Lutibacter sp. LPB0138, isolated from marine gastropod.";
RL   Submitted (OCT-2016) 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; CP017478; AOW19585.1; -; Genomic_DNA.
DR   RefSeq; WP_070235701.1; NZ_CP017478.1.
DR   AlphaFoldDB; A0A1D8P4T8; -.
DR   STRING; 1850246.LPB138_02335; -.
DR   KEGG; lul:LPB138_02335; -.
DR   OrthoDB; 9763983at2; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000176050; Chromosome.
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   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}; Reference proteome {ECO:0000313|Proteomes:UP000176050};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   494 AA;  55252 MW;  10D39CFA2650A19C CRC64;
     MQNKPNNITL VGAGIMSATL GVLLKKLMPN CKIDIYERLD KVGAESSDAW NNAGTGHAAY
     CELNYTPELE DGTIDISKAL KIGSSFEVSK QFWAYLKAEN HLPQSEAFIN DIAHMSFVWG
     EENIEFLKKR FEALTNCVLF EEMKYSEDLE EIEKWIPLMM HNRIDDEKIA VTRMEIGTDV
     NFGAITRGMI NYLQSCDGVE VHLGYNIDDL TKNKDGTWEI EMTDLATNKE KVVISDFVFI
     GAGGGSIPLL EKTDLEQGRG YAGFPVSGQW LKCTNPEVIQ QHEAKVYGKA STGSPPMSVP
     HLDTRMMNGK KALLFGPYAG FSTKFLKNGS YFDLPLSLEV HNIWPLLSAG IHNIDLTKYL
     IKQVVQSDEE RFAFLQKYFP DAKMEDWTLE HAGQRVQIIK KDEDEGGVLK FGTEIVTDDD
     GSLAALLGAS PGASTSVSIM LDVLDKCFPE AIASKEWQET LTTMIPSYGK SLVEHPELCR
     TIRERTTREL KLDD
//
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