ID B9C092_9BURK Unreviewed; 362 AA.
AC B9C092;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Phenylacetate-CoA oxygenase/reductase, PaaK subunit {ECO:0000313|EMBL:EEE03609.1};
GN Name=paaK {ECO:0000313|EMBL:EEE03609.1};
GN ORFNames=BURMUCGD2_0206 {ECO:0000313|EMBL:EEE03609.1};
OS Burkholderia multivorans CGD2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=513052 {ECO:0000313|EMBL:EEE03609.1, ECO:0000313|Proteomes:UP000004535};
RN [1] {ECO:0000313|EMBL:EEE03609.1, ECO:0000313|Proteomes:UP000004535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGD2 {ECO:0000313|EMBL:EEE03609.1,
RC ECO:0000313|Proteomes:UP000004535};
RX PubMed=23105085; DOI=10.1128/JB.01306-12;
RA Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., Radune D.,
RA Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., Greenberg D.E.,
RA Holland S.M., Goldberg J.B.;
RT "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic
RT Granulomatous Disease Burkholderia multivorans Isolates.";
RL J. Bacteriol. 194:6356-6357(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EEE03609.1}.
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DR EMBL; ACFC01000024; EEE03609.1; -; Genomic_DNA.
DR RefSeq; WP_006408270.1; NZ_ACFC01000024.1.
DR AlphaFoldDB; B9C092; -.
DR GeneID; 66525146; -.
DR Proteomes; UP000004535; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0010124; P:phenylacetate catabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06214; PA_degradation_oxidoreductase_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR011884; PaaE.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR NCBIfam; TIGR02160; PA_CoA_Oxy5; 1.
DR PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714}.
FT DOMAIN 4..112
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 271..362
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 362 AA; 40059 MW; C4DD28802477845D CRC64;
MATPQFHPLR IRDVRPETAD AVTVSFEVPP ELRDAYRFTQ GQFVTLKTHI DGEETRRSYS
ICVGTTDYDR DGELRIGIKR VRGGRFSNFA FDTLKPGHTI DVMTPDGRFF THLNADHGKQ
YVAFSGGSGI TPVLAIVKTT LELEPRSTFT LIYGNRSVDA IMFAEELEDL KNRYMNRFVL
YHVLSDDLQD VELFNGVLDQ AKCAAFLDTL VPADSIDEAF ICGPAPMMDA AEAALKAAGV
PPAKVHVERF GTPLPQAGVP VVEITEQTPA ADLEIVLDGK KRKLRLPYEG VSLLDVGLRA
GLALPYACKG GVCCTCRAKV LEGEVRMEKN YTLEEHEVND GFVLTCQCHP VSDRIVVSFD
ER
//
