ID A0A172YHV2_9GAMM Unreviewed; 502 AA.
AC A0A172YHV2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, 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=A5892_16290 {ECO:0000313|EMBL:ANF58828.1};
OS Halotalea alkalilenta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halotalea.
OX NCBI_TaxID=376489 {ECO:0000313|EMBL:ANF58828.1, ECO:0000313|Proteomes:UP000077875};
RN [1] {ECO:0000313|EMBL:ANF58828.1, ECO:0000313|Proteomes:UP000077875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHB B 13600 {ECO:0000313|EMBL:ANF58828.1,
RC ECO:0000313|Proteomes:UP000077875};
RA Swarnkar M.K., Sharma A., Kaushal K., Soni R., Rana S., Singh A.K.,
RA Gulati A.;
RT "Complete Genome Sequence of Halotalea alkalilenta IHB B 13600.";
RL Submitted (APR-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; CP015243; ANF58828.1; -; Genomic_DNA.
DR RefSeq; WP_064123684.1; NZ_CP015243.1.
DR AlphaFoldDB; A0A172YHV2; -.
DR STRING; 376489.A5892_16290; -.
DR KEGG; haa:A5892_16290; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000077875; 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:UP000077875};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
SQ SEQUENCE 502 AA; 55114 MW; B11BB4C622C4A519 CRC64;
MNQPATETAD VVLIGAGVMS ATLAVLLKEL DPEAKVEIVE QLDGAASESS FAWNNAGTGH
AALCELNYTP RNKDGSISIE KAVRINTAFE ESKQFWSYLI EQGAIESARR FLNPVPHMSF
VRGAKDVEFL RKRFEAMSAH PCFADMRYSE SPEQIAEWAP LLMRGRKGDD PIAATRVDQG
TDVDFGALTR QLLRHLDSLG GARVSYKQRV ASLEREANGD WLLELDVDHG KRSRQLRARF
VFVGAGGGAL PLLQKSGIPE AQGYAGFPVS GQWLRCDDPK LVAQHKAKVY SQASVGAPPM
SVPHLDTRVV DGRSSLLFGP FAGFTTKFLK TGSPLDLPLS VRADNLRPML SVARDNFSLV
KYLVGQVLQT PKQRIEALRE FFPEASEEDW RLEIAGQRVQ IIKRDAKRGG KLEFGTELVT
AADGSLAALL GASPGASTAV STMLQLIERC FPERYQSEDW QSRLGAIFTA RAGQLAQDGK
RLAEVRERTH RVLELTPQPA QA
//
