ID A0A0Q4C620_9SPHN Unreviewed; 449 AA.
AC A0A0Q4C620;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Benzoate 1,2-dioxygenase large subunit {ECO:0000313|EMBL:KQM20765.1};
GN ORFNames=ASE49_15780 {ECO:0000313|EMBL:KQM20765.1};
OS Novosphingobium sp. Leaf2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM20765.1, ECO:0000313|Proteomes:UP000050893};
RN [1] {ECO:0000313|EMBL:KQM20765.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM20765.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM20765.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM20765.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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:KQM20765.1}.
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DR EMBL; LMJY01000005; KQM20765.1; -; Genomic_DNA.
DR RefSeq; WP_056769001.1; NZ_LMJY01000005.1.
DR AlphaFoldDB; A0A0Q4C620; -.
DR STRING; 1735670.ASE49_15780; -.
DR OrthoDB; 7456916at2; -.
DR Proteomes; UP000050893; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd08879; RHO_alpha_C_AntDO-like; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 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:KQM20765.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000050893}.
FT DOMAIN 48..159
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 449 AA; 50719 MW; 855CF3D81594B8BF CRC64;
MQGHLMNRVA TAVVDDPETG LFRCRRDVFT DPALFELEMK YIFESNWVYV AHESQLEKKN
DYFTTWIGRT PVILTRGKDG GINCVVNACA HRGAKLCRRK RGNQPLFVCP FHGWSFKTDG
ALLRAKDAST GAYPDSFDHE GSHDLTRARV ESYRGFIFAS LNHDVRPLEQ HLGEAKVIID
QMVDQAPEGL EILTGNSTYT FDGNWKMQME NGCDGYHVSS VHENYQSTMG RRAEGGTKAV
DANGWSKAPA SGVYGFEHGH ILLWTQVLNP EVRPIWNHKA ALEERLGADK AKFILEQTRN
LALYPNVFLM DQFSTQIRVV RPIDVHTTEV TIYCYAPKGE SAQDRANRIR QYEDFFNVTG
MGTPDDLEEF RSCQKAYEGA GELWNDLSRG ATRWIAGPDA NAKAMGMNPL LSSERSEDEG
LFVRQHEFWA QIMLDGMAKD TEPMLEAAE
//
