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Database: UniProt
Entry: Q9PBD9_XYLFA
LinkDB: Q9PBD9_XYLFA
Original site: Q9PBD9_XYLFA 
ID   Q9PBD9_XYLFA            Unreviewed;       454 AA.
AC   Q9PBD9;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   OrderedLocusNames=XF_2205 {ECO:0000313|EMBL:AAF85004.1};
OS   Xylella fastidiosa (strain 9a5c).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=160492 {ECO:0000313|EMBL:AAF85004.1, ECO:0000313|Proteomes:UP000000812};
RN   [1] {ECO:0000313|EMBL:AAF85004.1, ECO:0000313|Proteomes:UP000000812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9a5c {ECO:0000313|EMBL:AAF85004.1,
RC   ECO:0000313|Proteomes:UP000000812};
RX   PubMed=10910347; DOI=10.1038/35018003;
RA   Simpson A.J., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA   Alvarenga R., Alves L.M., Araya J.E., Baia G.S., Baptista C.S.,
RA   Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.,
RA   Bueno M.R., Camargo A.A., Camargo L.E., Carraro D.M., Carrer H.,
RA   Colauto N.B., Colombo C., Costa F.F., Costa M.C., Costa-Neto C.M.,
RA   Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA   Facincani A.P., Ferreira A.J., Ferreira V.C., Ferro J.A., Fraga J.S.,
RA   Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA   Goldman M.H., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA   Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA   Laigret F., Lambais M.R., Leite L.C., Lemos E.G., Lemos M.V., Lopes S.A.,
RA   Lopes C.R., Machado J.A., Machado M.A., Madeira A.M., Madeira H.M.,
RA   Marino C.L., Marques M.V., Martins E.A., Martins E.M., Matsukuma A.Y.,
RA   Menck C.F., Miracca E.C., Miyaki C.Y., Monteriro-Vitorello C.B., Moon D.H.,
RA   Nagai M.A., Nascimento A.L., Netto L.E., Nhani A.Jr., Nobrega F.G.,
RA   Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C.,
RA   Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A., Pereira H.A.Jr.,
RA   Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de M Rosa A.J.,
RA   de Rosa V.E.Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.,
RA   da Silva A.M., da Silva F.R., da Silva W.A.Jr., da Silveira J.F.,
RA   Silvestri M.L., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F.,
RA   Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A.,
RA   Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J.,
RA   Setubal J.C.;
RT   "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL   Nature 406:151-159(2000).
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; AE003849; AAF85004.1; -; Genomic_DNA.
DR   PIR; A82587; A82587.
DR   AlphaFoldDB; Q9PBD9; -.
DR   STRING; 160492.XF_2205; -.
DR   KEGG; xfa:XF_2205; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_4_1_6; -.
DR   Proteomes; UP000000812; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
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;
FT   DOMAIN          28..207
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   454 AA;  50063 MW;  3AEBEF87A35BD0C9 CRC64;
     MHQTLPMLRL KTEPADLQHY GRDWTRRFTP APLAIALPAT VQEVQAIVRW ANDAHIAIVP
     SGGRTGLSGG AMATNGELVL SLERMNKMLR FDPMDRTMTV QAGMPLEAVQ AAARQHGLLY
     PVDFAARGSC SIGGTIATNA GGIRVVRYGN TREWIAGLNV VTGTGELLTL NHALIKNSSG
     YDFRHLMIGS EGTLGIVVEA TLRLTDPPPP TKVMLLALPT FDVLMQVFAA FRAQLQIEAF
     EFFTQRALPH VLAHGAQAPF EHPYPYYVVT EFPCADATQE TTALTVFETC MEQGWVLDGV
     ISQSDAQAAQ LWRLRESITE SIAPYTPYKN DIAVRIAAMP AFLEQAQTLL SQAYPEFEVL
     WFGHIGDGNL HINVLKPHTV PQADFIHTCE HVTALLADLL QRFRGSISAE HGIGLIKKPY
     LHSTRSPAEI ALMRQLKRAF DPKWILNPGK VFDP
//
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