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Database: UniProt
Entry: A0A101APZ1_9MYCO
LinkDB: A0A101APZ1_9MYCO
Original site: A0A101APZ1_9MYCO 
ID   A0A101APZ1_9MYCO        Unreviewed;       519 AA.
AC   A0A101APZ1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=AU194_04570 {ECO:0000313|EMBL:KUI26772.1};
OS   Mycobacterium sp. GA-2829.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1772283 {ECO:0000313|EMBL:KUI26772.1, ECO:0000313|Proteomes:UP000053444};
RN   [1] {ECO:0000313|EMBL:KUI26772.1, ECO:0000313|Proteomes:UP000053444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GA-2829 {ECO:0000313|EMBL:KUI26772.1,
RC   ECO:0000313|Proteomes:UP000053444};
RG   TB Trials Study Group;
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E.L., Macaden R.,
RA   Grewal H.M.S.;
RL   Submitted (JAN-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}.
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:KUI26772.1}.
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DR   EMBL; LQIT01000045; KUI26772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101APZ1; -.
DR   STRING; 1772283.AU194_04570; -.
DR   OrthoDB; 9763983at2; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000053444; 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   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:UP000053444};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
FT   REGION          493..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   519 AA;  56542 MW;  E90A823330107437 CRC64;
     MSDSQVAKTD VVLVGAGIMS ATLSVLLKQL EPNWTITLIE RLDGAAAESS FAWNNAGTGH
     SALCELNYTP EGPGGSIDIT KAVNVNEQFQ VSRQFWTHAV ENGVLPDVRN FINPVPHVSF
     VSGEKNRQYL RARYDALVTN PLFATMEYID DPDEFARRLP FMADKRDFRE PIALNWTQDG
     TDVDFGSLSR QLIGYSAQRG MTTLFGHEVR DLDKQSDGSW AVKVRNRRTG AKRKLNAKFV
     FVGAGGGALP LLQKAGIEEA KGFGGFPVGG QWLRSDNPEL TARHQAKVYG MPPLGAPPMS
     VPHLDTRVIN SKSYLLFGPF AGWSPKFLKQ GKVTDLPFSV RPNNLASMLG VGLTEMGLLK
     YLIGQLMLSE ADRVESLRDF APSARDADWE LDIAGQRVQV IRRKGRGGVL EFGTTVLAAK
     DGSIAGLLGA SPGASTAVPA MFDVMQRCFG DRYRAWEPKL KEIVPSLGTK LSDEPKLFEE
     IWAHGTKVLK LDRPAAGLPA TGSDTEHPTP DASRTTATA
//
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