AAAH_CHLPN
ID AAAH_CHLPN Reviewed; 362 AA.
AC Q9Z6L3;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable aromatic amino acid hydroxylase;
DE EC=1.14.16.-;
GN OrderedLocusNames=CPn_1046, CP_0806, CPj1046, CpB1086;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC hydroxylase family. {ECO:0000305}.
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DR EMBL; AE001363; AAD19183.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF73705.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA99253.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP99015.1; -; Genomic_DNA.
DR PIR; C86621; C86621.
DR PIR; E72002; E72002.
DR RefSeq; NP_225240.1; NC_000922.1.
DR AlphaFoldDB; Q9Z6L3; -.
DR SMR; Q9Z6L3; -.
DR STRING; 115711.CP_0806; -.
DR PRIDE; Q9Z6L3; -.
DR EnsemblBacteria; AAD19183; AAD19183; CPn_1046.
DR EnsemblBacteria; AAF73705; AAF73705; CP_0806.
DR KEGG; cpa:CP_0806; -.
DR KEGG; cpj:CPj1046; -.
DR KEGG; cpn:CPn_1046; -.
DR KEGG; cpt:CpB1086; -.
DR PATRIC; fig|115713.3.peg.1145; -.
DR eggNOG; COG3186; Bacteria.
DR HOGENOM; CLU_065322_0_0_0; -.
DR OrthoDB; 1492162at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016714; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR GO; GO:0009072; P:aromatic amino acid family metabolic process; IEA:InterPro.
DR Gene3D; 1.10.800.10; -; 1.
DR InterPro; IPR001273; ArAA_hydroxylase.
DR InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
DR InterPro; IPR036951; ArAA_hydroxylase_sf.
DR InterPro; IPR036329; Aro-AA_hydroxylase_C_sf.
DR InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
DR PANTHER; PTHR11473; PTHR11473; 1.
DR Pfam; PF00351; Biopterin_H; 1.
DR PRINTS; PR00372; FYWHYDRXLASE.
DR SUPFAM; SSF56534; SSF56534; 1.
DR PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE 3: Inferred from homology;
KW Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT CHAIN 1..362
FT /note="Probable aromatic amino acid hydroxylase"
FT /id="PRO_0000205577"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 205
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT CONFLICT 131
FT /note="E -> D (in Ref. 4; AAP99015)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 42513 MW; 01B89BB4B4FE593B CRC64;
MHYCERTLDP KYILKIALKL RQSLSLFFQN SQSLQRAYST PYSYYRIILQ KENKEKQALA
RHKCISILEF FKNLLFVHLL SLSKNQREGC STDMAVVSTP FFNRNLWYRL LSSRFSLWKS
YCPRFFLDYL EAFGLLSDFL DHQAVIKFFE LETHFSYYPV SGFVAPHQYL SLLQDRYFPI
ASVMRTLDKD NFSLTPDLIH DLLGHVPWLL HPSFSEFFIN MGRLFTKVIE KVQALPSKKQ
RIQTLQSNLI AIVRCFWFTV ESGLIENHEG RKAYGAVLIS SPQELGHAFI DNVRVLPLEL
DQIIRLPFNT STPQETLFSI RHFDELVELT SKLEWMLDQG LLESIPLYNQ EKYLSGFEVL
CQ