ID D4GFF9_PANAM Unreviewed; 549 AA.
AC D4GFF9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 79.
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 ECO:0000313|EMBL:ADD79279.1};
GN OrderedLocusNames=PANA_4112 {ECO:0000313|EMBL:ADD79279.1};
OS Pantoea ananatis (strain LMG 20103).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD79279.1, ECO:0000313|Proteomes:UP000001702};
RN [1] {ECO:0000313|EMBL:ADD79279.1, ECO:0000313|Proteomes:UP000001702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD79279.1,
RC ECO:0000313|Proteomes:UP000001702};
RX PubMed=20348253; DOI=10.1128/JB.00060-10;
RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA Coutinho T.A.;
RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT Eucalyptus blight and dieback.";
RL J. Bacteriol. 192:2936-2937(2010).
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; CP001875; ADD79279.1; -; Genomic_DNA.
DR RefSeq; WP_013027945.1; NC_013956.2.
DR AlphaFoldDB; D4GFF9; -.
DR STRING; 706191.PANA_4112; -.
DR KEGG; pam:PANA_4112; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_028151_0_0_6; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000001702; 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:UP000001702};
KW Signal {ECO:0000256|SAM:SignalP};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..549
FT /note="Probable malate:quinone oxidoreductase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003057883"
FT REGION 518..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 60041 MW; FDAA07209E200FE3 CRC64;
MIKSTKFVPA LSLAALLVSS VTHAENSPEK TDVLLIGGGI MSASLGTLLE ELQPGWKQIM
VEKLDGVALE SSNGWNNAGT GHSANMELNY TPERADGSID VTKALEINEA FMISRQFWSS
QVKDGVLNNP RSFINSTPHM SFVWGDNVDY LTKRYAALQK TVLFQGMKFS TDHKQIAQWA
PLVMEGRDPQ QKVAATWTPV GTDVNYGEIT RQLIGSLKKN DNFRLETSSE VTDFKRNSDN
SWHVTIKDAK NGGERTVDAK YVFIGAGGGA LKLLQKTGIP EADNYAGFPV GGSFLVTENS
AIADRHLAKV YGQASVGAPP MSVPHLDTRY LDGKRVVLFG PFATFSTKFL KNGSLFDLLS
TTTTHNFMPM THVGMDNFDL VKYLIGQVML SDDDRFAALK EYYPEAKKED WKLIQAGQRV
QIIKKDADKG GVLKLGTEIV TDQQKTVAAL LGASPGASTA APIAINVMQK LFPEQFKSAE
WQEKIRKIVP AYGQKLNDNP ALTQQVWDET AATLQLTKPP VIQMGNQPTE APAANSEKAP
VSAKHDMAL
//
