ID Q4KEJ2_PSEF5 Unreviewed; 473 AA.
AC Q4KEJ2;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=FAD binding domain protein {ECO:0000313|EMBL:AAY91507.1};
GN OrderedLocusNames=PFL_2234 {ECO:0000313|EMBL:AAY91507.1};
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:AAY91507.1, ECO:0000313|Proteomes:UP000008540};
RN [1] {ECO:0000313|EMBL:AAY91507.1, 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000076; AAY91507.1; -; Genomic_DNA.
DR RefSeq; WP_011060532.1; NC_004129.6.
DR AlphaFoldDB; Q4KEJ2; -.
DR STRING; 220664.PFL_2234; -.
DR KEGG; pfl:PFL_2234; -.
DR PATRIC; fig|220664.5.peg.2268; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_033233_0_0_6; -.
DR Proteomes; UP000008540; 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 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; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR13878:SF91; L-GULONOLACTONE OXIDASE 3; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..473
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004240201"
FT DOMAIN 32..200
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 473 AA; 52471 MW; 341BDE41258DE521 CRC64;
MRFAIGLFLC AALGGALTTH AAETVNDITQ LNPIVVDQVV RPTRLEQIVQ LVAGHPGPIA
IGGGRYSMGG QTATEQALQI DMRGFNRVLD FSKERKEITV QPGITWRAVQ DYIDPHDLSV
SIMQSYANFT VGGALSVNAH GRYIGYGPLV SSVKSIKLVL ADGQVVDASP QHNSDLFYGA
IGGYGGLGVI VQATLQLSDN VRLLRSVDEM PLGDYRPYFQ ARIQNNPKVI LHNAVLYPDQ
YQTLRAVSYS QTDLPVTVKE RLTPLDQNYW KEQKALKVVS QWPGGKTLRQ EVIDPLVLKK
PQVSWRNHEA SLDVRELEPD SRAKRTYVLQ EYFVPPDQLE SFVQEMGATL RAHKVNVINL
SIRHAKADPG TLLAWAKTEV FALVLYYQQS TAPEEREKVG VWTRALVDSA IERGGSYYLP
YQIHATAQQF RAAYPRAGEF LALKARVDPQ NKFRNKLWDA YGLGATGDGA AQP
//
