ID A0A241W0Y2_9GAMM Unreviewed; 471 AA.
AC A0A241W0Y2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Anthranilate 1,2-dioxygenase large subunit {ECO:0000313|EMBL:OTG87391.1};
GN ORFNames=B9T31_02495 {ECO:0000313|EMBL:OTG87391.1};
OS Acinetobacter sp. ANC 4558.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1977876 {ECO:0000313|EMBL:OTG87391.1, ECO:0000313|Proteomes:UP000194907};
RN [1] {ECO:0000313|EMBL:OTG87391.1, ECO:0000313|Proteomes:UP000194907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 4558 {ECO:0000313|EMBL:OTG87391.1,
RC ECO:0000313|Proteomes:UP000194907};
RA Nemec A., Radolfova-Krizova L.;
RT "High diversity of culturable Acinetobacter species in natural soil and
RT water ecosystems.";
RL Submitted (APR-2017) 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:OTG87391.1}.
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DR EMBL; NEGH01000002; OTG87391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A241W0Y2; -.
DR STRING; 1977876.B9T31_02495; -.
DR OrthoDB; 9769355at2; -.
DR Proteomes; UP000194907; 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 CDD; cd03469; Rieske_RO_Alpha_N; 1.
DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR InterPro; IPR017638; Anthranilate_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; TIGR03228; anthran_1_2_A; 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, ECO:0000313|EMBL:OTG87391.1};
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}.
FT DOMAIN 52..160
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 471 AA; 54063 MW; 91A24326429D215E CRC64;
MASSNLKQWN DFIEGCIDFR PQDGVYKIAR DMFTQPELFE LEMELIFEKA WIYACHESEI
PNNHDFITVQ IGRQPMIISR DGQGQLHAMV NACEHRGATL TRVAKGNQST FTCPFHAWCY
KSDGRLVKVK APSEYCEDFD KASRGLKQGR IESYRGFVFV SLDTQATDTL EEFLGDAKLF
IDLMVNQSPT GELEVLQGKS AYTFAGNWKL QNENGLDGYH VSTVHYNYVS TVQHRQQVNI
ANGSELDTLD YSKLGAGDNE TDDGWFSFKN GHSVLFSDMP NPTVRPGYST VMPYMVEKYG
EKYAEWAMHR LRNLNLYPSL FFMDQISSQL RIIRPVAWNK TEVVSQCIGV KGESAEARRN
RIRQFEDFFN VSGLGTPDDL VEFREQQRGF QARLERWSDI SRGHQHWEYG ATKNSQDLNI
HPVITGREIT HEGLYINQHG HWKNLMLKGL NNKALKMQDI TFENNALVDE V
//
