ID A1K6L2_AZOSB Unreviewed; 353 AA.
AC A1K6L2;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Phenol 2-monooxygenase {ECO:0000313|EMBL:CAL94467.1};
DE EC=1.14.13.7 {ECO:0000313|EMBL:CAL94467.1};
GN Name=lapP {ECO:0000313|EMBL:CAL94467.1};
GN OrderedLocusNames=azo1850 {ECO:0000313|EMBL:CAL94467.1};
OS Azoarcus sp. (strain BH72).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699 {ECO:0000313|EMBL:CAL94467.1, ECO:0000313|Proteomes:UP000002588};
RN [1] {ECO:0000313|EMBL:CAL94467.1, ECO:0000313|Proteomes:UP000002588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72 {ECO:0000313|EMBL:CAL94467.1,
RC ECO:0000313|Proteomes:UP000002588};
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AM406670; CAL94467.1; -; Genomic_DNA.
DR RefSeq; WP_011765583.1; NC_008702.1.
DR AlphaFoldDB; A1K6L2; -.
DR STRING; 62928.azo1850; -.
DR KEGG; azo:azo1850; -.
DR eggNOG; COG2871; Bacteria.
DR HOGENOM; CLU_003827_7_0_4; -.
DR Proteomes; UP000002588; Chromosome.
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:0018662; F:phenol 2-monooxygenase activity; IEA:UniProtKB-EC.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06211; phenol_2-monooxygenase_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; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
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};
KW Oxidoreductase {ECO:0000313|EMBL:CAL94467.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002588}.
FT DOMAIN 3..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 102..203
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 353 AA; 38649 MW; DD12EFBF831171BB CRC64;
MSYELTIEPL GQTIAIEEGQ TILDAALRAG IYLPHACCHG LCATCKVQVV DGEVEHGAAS
SFALMDFERD EQKCLACCAT AESDLVIEAE IEDDPDALNL PVRDFDGVVS RIESLTPTIK
GVWVKLDEPE GMRFQAGQYI NLHLPDGIGT RAFSIASAPS AAGEIELNIR IVAGGQGTAY
VHEKLKAGDA IRITGPYGRF FVKKSAKVPV VFMAGGSGLS SPRSMILDLL EEGFDLPITL
VYGQRSRAEL YYHDEFLALA QRHPNFRYVP ALSHEPEGSD WNGFRGFVHE AAKAAFDNDF
RGHKAYLCGP PLMIDACITT LMQGRLFERD IYMEKFISAA DAQQVRSPLF KAI
//