ID A0A0T1WEM0_9MYCO Unreviewed; 458 AA.
AC A0A0T1WEM0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Benzoate 1,2-dioxygenase large subunit {ECO:0000313|EMBL:KQY07578.1};
GN ORFNames=ASD37_11540 {ECO:0000313|EMBL:KQY07578.1};
OS Mycobacterium sp. Root135.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1736457 {ECO:0000313|EMBL:KQY07578.1, ECO:0000313|Proteomes:UP000051127};
RN [1] {ECO:0000313|EMBL:KQY07578.1, ECO:0000313|Proteomes:UP000051127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root135 {ECO:0000313|EMBL:KQY07578.1,
RC ECO:0000313|Proteomes:UP000051127};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY07578.1, ECO:0000313|Proteomes:UP000051127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root135 {ECO:0000313|EMBL:KQY07578.1,
RC ECO:0000313|Proteomes:UP000051127};
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 -!- 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}.
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:KQY07578.1}.
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DR EMBL; LMEZ01000005; KQY07578.1; -; Genomic_DNA.
DR RefSeq; WP_056553088.1; NZ_LMEZ01000005.1.
DR AlphaFoldDB; A0A0T1WEM0; -.
DR STRING; 1736457.ASD37_11540; -.
DR OrthoDB; 5243643at2; -.
DR Proteomes; UP000051127; 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 GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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; 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.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Dioxygenase {ECO:0000313|EMBL:KQY07578.1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000051127}.
FT DOMAIN 54..151
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 458 AA; 51267 MW; 009834D613BB178E CRC64;
MTTSIEPTNR VETVLANAVV DDAEAGVYRT NRKIFTDEEI FELEIKHIFE GNWIYLAHES
QVANPGDYFT TYIGRQPVVI TRDKNGNLNC LINACAHRGA MICRRKTDNR MTLTCPFHGW
TFRNDGALLK VKDPEGAGYP ETFNSGGSHD MTKVARFEGY RGFLFGSLND DVLPLAEHLG
DATKVIDMLV DQSPDGLEVL RGSSTYTYDG NWKVQAENGA DGYHVTATHW NYAATTSRRT
TGESTNDTKA LDAGSWGKSG GGYWSFPHGH LCLWTWAGNP QDRPLWDKLD DLKSTFGDAK
GEFMVKGSRN LCVYPNVYVM DQFSTQIRHF RPIAPDKTEV TIYCIAPKGE SDTARSHRIR
QYEDFFNASG MATPDDLEEF RSCQLTFRAE AAPWNDMSRG AEHWLTGPDE VARSLDMDGV
ISSGVKNEDE GLYPVQHGYW LDTLRNALGR EQDKGMGA
//
