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Database: UniProt
Entry: A0A099PBC7_9GAMM
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ID   A0A099PBC7_9GAMM        Unreviewed;       353 AA.
AC   A0A099PBC7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Phenol hydroxylase {ECO:0000313|EMBL:KGK41346.1};
GN   ORFNames=LH51_15340 {ECO:0000313|EMBL:KGK41346.1};
OS   Nitrincola sp. A-D6.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Nitrincola.
OX   NCBI_TaxID=1545442 {ECO:0000313|EMBL:KGK41346.1, ECO:0000313|Proteomes:UP000029924};
RN   [1] {ECO:0000313|EMBL:KGK41346.1, ECO:0000313|Proteomes:UP000029924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-D6 {ECO:0000313|EMBL:KGK41346.1,
RC   ECO:0000313|Proteomes:UP000029924};
RA   Valdes N., Rivera-Araya J., Bijman J., Escudero G L., Demergasso C.,
RA   Fernandez S., Ferrer A., Chavez R., Levican G.;
RT   "Draft Genome Sequence of the Arsenic-Resistant Bacterium Nitrincola sp.
RT   Strain A-D6 Isolated from a Salt Flat in Northern Chile.";
RL   Submitted (SEP-2014) 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:KGK41346.1}.
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DR   EMBL; JRLB01000094; KGK41346.1; -; Genomic_DNA.
DR   RefSeq; WP_036523540.1; NZ_JRLB01000094.1.
DR   AlphaFoldDB; A0A099PBC7; -.
DR   STRING; 1545442.LH51_15340; -.
DR   OrthoDB; 9806195at2; -.
DR   Proteomes; UP000029924; 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   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; IPR006058; 2Fe2S_fd_BS.
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; PS00197; 2FE2S_FER_1; 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   Reference proteome {ECO:0000313|Proteomes:UP000029924}.
FT   DOMAIN          3..93
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          102..201
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   353 AA;  38395 MW;  99D7905602EC5BB3 CRC64;
     MTYAVTVEPT GDVIEVEEGQ TILDAALRQG VWLPFACGHG TCATCKVQVV EGDVEIGNAS
     PFALMDVERD EGKVLACCAI PESDLVIEAD VDVDPDFAGY PVEDFNATVV SIQDLSPSIK
     EIRVALDRPM TFQAGQYVNL NLPGVEGSRA FSIANPPSDD RHIELHVRLV PGGAATTWLH
     ESLQPGDELD LSGPYGQFFV RKSDAKDVIF IAGGSGLSSP QSMILDLLEQ GDTRQIYLFQ
     GARNLSELYN RERLEALTRT HANFHYIPAL NEPTEADGWT GFAGFVHEAA KDFFDGRFNG
     HKAYLCGPPP MIDAAISTLM LGRVFEADIH MEKFLTAADG ASAETRSALF KRI
//
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