ID A0A1C3CXK0_9GAMM Unreviewed; 461 AA.
AC A0A1C3CXK0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Benzoate 1,2-dioxygenase large subunit {ECO:0000313|EMBL:ODA13413.1};
GN ORFNames=BBP83_03200 {ECO:0000313|EMBL:ODA13413.1};
OS Acinetobacter celticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1891224 {ECO:0000313|EMBL:ODA13413.1, ECO:0000313|Proteomes:UP000186553};
RN [1] {ECO:0000313|EMBL:ODA13413.1, ECO:0000313|Proteomes:UP000186553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 4603 {ECO:0000313|EMBL:ODA13413.1,
RC ECO:0000313|Proteomes:UP000186553};
RA Radolfova-Krizova L., Nemec A.;
RT "Acinetobacter sp. ANC 4603.";
RL Submitted (JUL-2016) 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:ODA13413.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MBDL01000008; ODA13413.1; -; Genomic_DNA.
DR RefSeq; WP_068886175.1; NZ_MBDL01000008.1.
DR AlphaFoldDB; A0A1C3CXK0; -.
DR STRING; 1891224.BBP83_03200; -.
DR OrthoDB; 9769355at2; -.
DR Proteomes; UP000186553; 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; IPR017639; Benzo_1-2-diOase_lsu.
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 NCBIfam; TIGR03229; benzo_1_2_benA; 1.
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};
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}.
FT DOMAIN 54..136
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 461 AA; 52516 MW; A948ED49F7DF1898 CRC64;
MPRIPVINTS HLDRIDELLV DNFETGEFKL HRSVFTDQAL FDLEMKYIFE GNWVYLAHES
QIPNNNDFYT TYIGRQPIII ARNRTGELNA MINACSHRGA QICRNKRGNK ATYTCPFHGW
TFNNSGKLLK VKDPADAGYS DCFNQEGSHD LKKVARFESY KGFLFGSLNP DVPTLEEFLG
ETTKIIDMIV DQSEQGLEIL RGSSTYTYDG NWKLTAENGA DGYHVSAVHW NYAATTQQRK
EKEAADNVRA MSAGSWGKQG GGSYGFEHGH MLLWTQWANP EDRPNFPKAD EYTEKFGAPM
SKWMIERSRN LCLYPNVYFM DQFGSQIRVL RPISVNKTEV TIYCIAPIGE DKESRTRRIR
QYEDFFNASG MATPDDLEEF RACQAGYAGI ELEWNDMCRG SKHWVHGPDE AADEIGLKPL
LSCIKTEDEG LYLAQHQYWL KTMKHAIASE KELATTEGES A
//
