ID A0A0H4WQN6_9BORD Unreviewed; 325 AA.
AC A0A0H4WQN6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Anthranilate 1,2-dioxygenase large subunit {ECO:0000313|EMBL:AKQ57483.1};
DE EC=1.14.12.1 {ECO:0000313|EMBL:AKQ57483.1};
GN Name=antA {ECO:0000313|EMBL:AKQ57483.1};
GN ORFNames=ACR54_04204 {ECO:0000313|EMBL:AKQ57483.1};
OS Bordetella hinzii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=103855 {ECO:0000313|EMBL:AKQ57483.1, ECO:0000313|Proteomes:UP000036382};
RN [1] {ECO:0000313|EMBL:AKQ57483.1, ECO:0000313|Proteomes:UP000036382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F582 {ECO:0000313|EMBL:AKQ57483.1,
RC ECO:0000313|Proteomes:UP000036382};
RX PubMed=26316634;
RA Weigand M.R., Changayil S., Kulasekarapandian Y., Tondella M.L.;
RT "Complete Genome Sequences of Two Bordetella hinzii Strains Isolated from
RT Humans.";
RL Genome Announc. 3:e00965-e00915(2015).
RN [2] {ECO:0000313|Proteomes:UP000036382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F582 {ECO:0000313|Proteomes:UP000036382};
RA Weigand M.R., Changayil S., Kulasekarapandian Y., Batra D., Williams M.M.,
RA Tondella M.L.;
RT "Complete Genome Sequences of Two Bordetella hinzii Isolated from Humans.";
RL Submitted (JUL-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}.
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DR EMBL; CP012076; AKQ57483.1; -; Genomic_DNA.
DR RefSeq; WP_029580070.1; NZ_CP012076.1.
DR AlphaFoldDB; A0A0H4WQN6; -.
DR STRING; 103855.ACR54_04204; -.
DR KEGG; bhz:ACR54_04204; -.
DR PATRIC; fig|103855.15.peg.4175; -.
DR eggNOG; COG4638; Bacteria.
DR Proteomes; UP000036382; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018618; F:anthranilate 1,2-dioxygenase (deaminating, decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR CDD; cd00680; RHO_alpha_C; 1.
DR CDD; cd03469; Rieske_RO_Alpha_N; 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; CHOLINE MONOOXYGENASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43756:SF5; 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:0000313|EMBL:AKQ57483.1};
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:AKQ57483.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036382}.
FT DOMAIN 29..140
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 325 AA; 37511 MW; 1A7DF7D7E8435260 CRC64;
MKQAVFKPEW YVSPEYAEYE RVRLFEKLWL AAGFSSAIRN NGDYFVLMIH GQRVLVHRLG
GEIVAYVDAC PHRGGVIATA ERGNTRPVCK YHGWAFREGR ELTGVPMASQ FEHDGALRDR
SCGRRLKPLA VHCVGPLIFV NLAEQPLPFE EQFSAELIAW FERMGQTSAM IQLSFKCDFN
WKLNAENVRD SLHPFFVHAD SFSPVLPKAT EAFSQDRMVR LRPTEGEDWP RHEMPIPALR
ELSYVWTPEF DEGSYWYDGL LRRSLPQDRF VDMLLFPNTN LYSVGGRYYG LQQYLPTSAT
TFDYRLIESG VIRDSLVADE IRVLR
//
