ID B0VPS2_ACIBS Unreviewed; 471 AA.
AC B0VPS2;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Anthranilate dioxygenase large subunit {ECO:0000313|EMBL:CAP01305.1};
DE EC=1.14.12.1 {ECO:0000313|EMBL:CAP01305.1};
GN Name=antA {ECO:0000313|EMBL:CAP01305.1};
GN OrderedLocusNames=ABSDF1971 {ECO:0000313|EMBL:CAP01305.1};
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP01305.1, ECO:0000313|Proteomes:UP000001741};
RN [1] {ECO:0000313|EMBL:CAP01305.1, ECO:0000313|Proteomes:UP000001741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF {ECO:0000313|EMBL:CAP01305.1,
RC ECO:0000313|Proteomes:UP000001741};
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000256|ARBA:ARBA00008751}.
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DR EMBL; CU468230; CAP01305.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VPS2; -.
DR KEGG; abm:ABSDF1971; -.
DR HOGENOM; CLU_026244_4_1_6; -.
DR Proteomes; UP000001741; 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; 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:CAP01305.1};
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:CAP01305.1}.
FT DOMAIN 52..160
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
SQ SEQUENCE 471 AA; 53893 MW; B3C7A474A2800210 CRC64;
MTSSNLKQWN DFIDGCIDFR PNDGVFRIAR NMFTEPELFD LEMEFIFEKV WIYACHESEI
PNNHDFLTVQ IGRQPIIVSR DGKGELHAMV NACEHRGATL TRVAKGNQST FTCPFHAWCY
KSDGRLVKVK APSEYCEDFD KSSRGLKQGR IASYRGFVFV SLDTQATDSL EDFLGDAKLF
LDLMVNQSPT GELEVLQGKS SYTFAGNWKL QNENGLDGYH VSTVHYNYVS TVQHRQQVNA
SKGAELDTLN YSKLGAGDSE TDDGWFSFKN GHSVLFSDMP NPTVRPGYST VMPYMVEKYG
EKYAEWAMHR LRNLNLYPSL FFMDQISSQL RIVRPVAWNK TEVISQCIGV KGESTEARRN
RIRQFEDFFN VSGLGTPDDL VEFREQQKGF QARLERWSDI SRGCQSWEYG ATKNSQDLGI
QPVITGREFT HEGLYVNQHG LWQRLMLDGL NKKALKMQDI TFENNAVMDE V
//
