ID Q4KEF7_PSEF5 Unreviewed; 499 AA.
AC Q4KEF7;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:AAY91542.1};
GN Name=glcD {ECO:0000313|EMBL:AAY91542.1};
GN OrderedLocusNames=PFL_2269 {ECO:0000313|EMBL:AAY91542.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY91542.1, ECO:0000313|Proteomes:UP000008540};
RN [1] {ECO:0000313|EMBL:AAY91542.1, ECO:0000313|Proteomes:UP000008540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC {ECO:0000313|Proteomes:UP000008540};
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000076; AAY91542.1; -; Genomic_DNA.
DR RefSeq; WP_011060567.1; NC_004129.6.
DR AlphaFoldDB; Q4KEF7; -.
DR STRING; 220664.PFL_2269; -.
DR KEGG; pfl:PFL_2269; -.
DR PATRIC; fig|220664.5.peg.2306; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_6; -.
DR Proteomes; UP000008540; Chromosome.
DR GO; GO:0009339; C:glycolate oxidase complex; IEA:InterPro.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase 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 Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR004490; GlcD.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR00387; glcD; 1.
DR PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF1; GLYCOLATE OXIDASE SUBUNIT GLCD; 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 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827}.
FT DOMAIN 52..230
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 499 AA; 53925 MW; 9BF1D555C3795B14 CRC64;
MTILYDERLD GALPDVDRQA LIQALRQQLP ELELLDQEQQ LKPYECDGLS AYRSTPMLVA
LPRHLDQVQR ILQICHAHRV PVVARGAGTG LSGGALPLEK GLLLVMARFK EILQIDPAAR
CARLQPGVRN LAISQAAAPF GLYYAPDPSS QIACSIGGNV AENAGGVHCL KYGLTVHNLL
KVQMLSVEGQ PLTLGSEALD APGFDLLALF TGSEGLLGVI TEVTVKLLPK PQIAKVLLAA
FDSVEAAGRA VADIIAAGII PGGLEMMDNL AIRAAEDFIH AGYPVDAEAI LLCELDGVEA
DVHDDCERVR QVLERAGASE VRLARDEAER VRFWAGRKNA FPAVGRLSPD YYCMDGTIPR
RELPGVLRGI ARLADEHQLR VANVFHAGDG NMHPLILFDA NQPGELERAE ALGGKILELC
VAVGGSITGE HGVGREKINQ MCAQFNHHEL TLFHAIKAAF DPSGLLNPGK NIPTLHRCAE
FGAMHIHHGQ LPFPELERF
//
