ID Q87C42_XYLFT Unreviewed; 462 AA.
AC Q87C42;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 105.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:AAO29103.1};
GN OrderedLocusNames=PD_1254 {ECO:0000313|EMBL:AAO29103.1};
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190 {ECO:0000313|EMBL:AAO29103.1, ECO:0000313|Proteomes:UP000002516};
RN [1] {ECO:0000313|EMBL:AAO29103.1, ECO:0000313|Proteomes:UP000002516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964 {ECO:0000313|Proteomes:UP000002516};
RX PubMed=12533478; DOI=10.1128/JB.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E., da Silva A.C., Moon D.H., Takita M.A.,
RA Lemos E.G., Machado M.A., Ferro M.I., da Silva F.R., Goldman M.H.,
RA Goldman G.H., Lemos M.V., El-Dorry H., Tsai S.M., Carrer H., Carraro D.M.,
RA de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L., Kimura E.T.,
RA Ferro E.S., Harakava R., Kuramae E.E., Marino C.L., Giglioti E.,
RA Abreu I.L., Alves L.M., do Amaral A.M., Baia G.S., Blanco S.R., Brito M.S.,
RA Cannavan F.S., Celestino A.V., da Cunha A.F., Fenille R.C., Ferro J.A.,
RA Formighieri E.F., Kishi L.T., Leoni S.G., Oliveira A.R., Rosa V.E.Jr.,
RA Sassaki F.T., Sena J.A., de Souza A.A., Truffi D., Tsukumo F., Yanai G.M.,
RA Zaros L.G., Civerolo E.L., Simpson A.J., Almeida N.F.Jr., Setubal J.C.,
RA Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; AE009442; AAO29103.1; -; Genomic_DNA.
DR RefSeq; WP_004088327.1; NC_004556.1.
DR AlphaFoldDB; Q87C42; -.
DR GeneID; 58016786; -.
DR KEGG; xft:PD_1254; -.
DR HOGENOM; CLU_017779_4_1_6; -.
DR OMA; ITECEAH; -.
DR Proteomes; UP000002516; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002516}.
FT DOMAIN 36..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 462 AA; 50948 MW; EB66F61517BAF287 CRC64;
MNDSRLTSLH QTLPTLRLKT EPADLQHYGR DWTRRFTPAP LAIALPATVQ EVQAIVRWAN
DAHIAIVPSG GRTGLSGGAM ATNGELVLSL ERMNKMLQFD PMDRTMTVQA GMPLEAVQAV
ARQHGLLYPV DFAARGSCSI GGTIATNAGG IRVVRYGNTR EWIAGLNVVT GTGELLELNH
ALIKNSSGYD FRHLMIGSEG TLGIVVEATL RLTDPPPPTK VMLLALPTFD VLMQVFAAFR
AQLQIEAFEF FTQRALPHVL AHGAQAPFEH PYPYYVVTEF PCADAAQETT ALTVFETCME
QGWVLDGVIS QSDAQAAQLW RLRESITESI APYTPYKNDI AVRIAAMPAF LEQAQTLLSQ
AYPEFEVLWF GHIGDGNLHI NVLKPHTVPQ TDFIHTCEHV TALLADLLQR FRGSISAEHG
IGLIKKPYLH STRSPAEIAL MRQLKRAFDP KWILNPGKVF DP
//