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Database: UniProt
Entry: A0A0Q4GP48_9BURK
LinkDB: A0A0Q4GP48_9BURK
Original site: A0A0Q4GP48_9BURK 
ID   A0A0Q4GP48_9BURK        Unreviewed;       323 AA.
AC   A0A0Q4GP48;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=ASE76_05230 {ECO:0000313|EMBL:KQM75360.1};
OS   Xylophilus sp. Leaf220.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Xylophilus.
OX   NCBI_TaxID=1735686 {ECO:0000313|EMBL:KQM75360.1, ECO:0000313|Proteomes:UP000051325};
RN   [1] {ECO:0000313|EMBL:KQM75360.1, ECO:0000313|Proteomes:UP000051325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf220 {ECO:0000313|EMBL:KQM75360.1,
RC   ECO:0000313|Proteomes:UP000051325};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQM75360.1, ECO:0000313|Proteomes:UP000051325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf220 {ECO:0000313|EMBL:KQM75360.1,
RC   ECO:0000313|Proteomes:UP000051325};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQM75360.1}.
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DR   EMBL; LMKO01000012; KQM75360.1; -; Genomic_DNA.
DR   RefSeq; WP_055838077.1; NZ_LMKO01000012.1.
DR   AlphaFoldDB; A0A0Q4GP48; -.
DR   STRING; 1735686.ASE76_05230; -.
DR   OrthoDB; 9814706at2; -.
DR   Proteomes; UP000051325; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 2.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   PANTHER; PTHR42659:SF5; ALDEHYDE OXIDOREDUCTASE FAD-BINDING SUBUNIT PAOB-RELATED; 1.
DR   PANTHER; PTHR42659; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051325}.
FT   DOMAIN          1..222
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   323 AA;  34160 MW;  FC4DBC4D94976A5E CRC64;
     MKQFSYDRAD SIESAAQMLA SRPDTKLIAG GTNLLDLMKL QIETPAHLVD VSRLPLAGID
     ATPEGGVRIG AMVRNSALAA DPRIRRDYPL LSRALLSGAS AQLRNKATTG GNLLQRTRCP
     YFYDTHMPCN KRKPGSGCAA IGGVNRIHAI LGASEACIAV HPSDMAVAMH ALDAQVETHG
     PSGRRTIPIA DFHRLPGNEP ERDSNLGPQD VITAVVLPAP VGGRQIYRKV RDRASYAFAL
     ISVAAIVQPQ GGKTGSVLAL GGVAHKPWRQ PAAEAAIRDG SAGKWTAATD ALLAGAKGQG
     HNDFKIPLVR RTVTAVLDEA TRA
//
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