ID A0A126Z3L9_9MICO Unreviewed; 476 AA.
AC A0A126Z3L9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=AX769_18580 {ECO:0000313|EMBL:AMM21788.1};
OS Frondihabitans sp. PAMC 28766.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=1795630 {ECO:0000313|EMBL:AMM21788.1, ECO:0000313|Proteomes:UP000070552};
RN [1] {ECO:0000313|EMBL:AMM21788.1, ECO:0000313|Proteomes:UP000070552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC28744 {ECO:0000313|Proteomes:UP000070552};
RA Park H.;
RT "Complete genome of Frondihabitans sp.";
RL Submitted (FEB-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; CP014513; AMM21788.1; -; Genomic_DNA.
DR RefSeq; WP_066282189.1; NZ_CP014513.1.
DR AlphaFoldDB; A0A126Z3L9; -.
DR STRING; 1795630.AX769_18580; -.
DR KEGG; frp:AX769_18580; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000070552; 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:UP000070552};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
SQ SEQUENCE 476 AA; 51752 MW; AFBAFA04A5215286 CRC64;
MSATLGALLK QLQPDWTIRV YEALNDVAQE SSNPWNNAGT GHSALCELNY TPEKGDGSID
ITSAVKVNEQ FQVSRQFWSY LVDKGALPQP DQFINSTPHM SFVWGADNVE YLRKRYEALK
DHPLFQGMEF SDDPGQIAKW APSLVPGRTK AQPIAATHIL AGTDVDFGSL TRSLLRYLTE
NGVDLALGNR VTNLSRNRDR TWRIDLAVGA TAEPVRVNAR FVFVGAGGGA LNLLQKSGIP
EIRGFGGFPV SGEFLRTDNP AVVAKHQAKV YGKASVGAPP MSVPHLDTRV VDGSSSLMFG
PYAGFSPKFL KSGSYLDLFR SIRLHNLYPM IRVALSNVDL LKYLIGQLAA SKRTKFDALK
EFMPDADPRD WYRITAGQRV QVIKADKEKG GVLQFGTEVV AAKDGSIAGL LGASPGASTA
VPIMLTILDR CFPAKRDEWA PQLKAMIPTI GQQLAADEKQ AAATMGSTAE ALHIHV
//
