ID S5GAZ4_9NOCA Unreviewed; 271 AA.
AC S5GAZ4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Biphenyl 2,3-dioxygenase alpha subunit {ECO:0000313|EMBL:AGQ53946.1};
DE EC=1.14.12.18 {ECO:0000313|EMBL:AGQ53946.1};
DE Flags: Fragment;
GN Name=bphA1 {ECO:0000313|EMBL:AGQ53946.1};
OS Rhodococcus sp. P20.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1356634 {ECO:0000313|EMBL:AGQ53946.1};
RN [1] {ECO:0000313|EMBL:AGQ53946.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P20 {ECO:0000313|EMBL:AGQ53946.1};
RA Shumkova E.S., Egorova D.O., Korsakova E.S., Dorofeeva L.V.,
RA Plotnikova E.G.;
RT "Molecular Biological Characterization of Biphenyl-Degrading Bacteria and
RT Identification of the Biphenyl 2,3-Dioxygenase alpha-Subunit Genes.";
RL Microbiology (Mosc.) 83:160-168(2014).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; KC832467; AGQ53946.1; -; Genomic_DNA.
DR AlphaFoldDB; S5GAZ4; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018687; F:biphenyl 2,3-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR Gene3D; 2.20.25.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756:SF1; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43756; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF55961; Bet v1-like; 1.
DR SUPFAM; SSF50022; ISP domain; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000313|EMBL:AGQ53946.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AGQ53946.1}.
FT DOMAIN 1..74
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGQ53946.1"
FT NON_TER 271
FT /evidence="ECO:0000313|EMBL:AGQ53946.1"
SQ SEQUENCE 271 AA; 30206 MW; 5FA7358A069FE4DF CRC64;
RVFLNQCRHR GMRICRADGG NAKSFTCSYH GWAYDTGGNL VSVPFEEQAF PGLRKEDWGP
LQARVETYKG LIFANWDADA PDLDTYLGEA KFYMDHMLDR TEAGTEAIPG IQKWVIPCNW
KFAAEQFCSD MYHAGTTSHL SGILAGLPDG VDLSELAPPT EGIQYRATWG GHGSGFYIGD
PNLLVAVMGP KVTEYWTQGT AAEKASERLG STERGQQLMT QHMTIFPTCS FLPGINTIRA
WHPRGPNEIE VWAFTVVDAD APDEMKEEYR Q
//
