ID CP53_ASPNG STANDARD; PRT; 517 AA. AC P17549; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 25-JAN-2005 (Rel. 46, Last annotation update) DE Benzoate 4-monooxygenase (EC 1.14.13.12) (Benzoate-para-hydroxylase) DE (Cytochrome P450 53) (BpH). GN Name=bphA; Synonyms=cyp53, cyp53A1; OS Aspergillus niger. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus. OX NCBI_TaxID=5061; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 1055 / DSM 2061; RX MEDLINE=91066829; PubMed=2250647; RA van Gorcom R.F.M., Boschloo J.G., Kuijvenhoven A., Lange J., RA van Vark A.J., Bos C.J., van Balken J.A.M., Pouwels P.H., RA van den Hondel C.A.M.J.J.; RT "Isolation and molecular characterisation of the benzoate-para- RT hydroxylase gene (bphA) of Aspergillus niger: a member of a new gene RT family of the cytochrome P450 superfamily."; RL Mol. Gen. Genet. 223:192-197(1990). RN [2] RP NUCLEOTIDE SEQUENCE. RA Higgins U.M., Darby R.M., Maddison A., Lamb D.C., Draper J.; RT "Yeast heterologous expression of a benzoate 4-hydroxylase (CYP53) RT from Aspergillus niger."; RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP CHARACTERIZATION. RC STRAIN=T18.5; RX MEDLINE=21478854; PubMed=11594739; DOI=10.1006/abbi.2001.2534; RA Faber B.W., van Gorcom R.F.M., Duine J.A.; RT "Purification and characterization of benzoate-para-hydroxylase, a RT cytochrome P450 (CYP53A1), from Aspergillus niger."; RL Arch. Biochem. Biophys. 394:245-254(2001). CC -!- FUNCTION: Responsible for cytochrome P450 dependent benzoate CC hydroxylation in microsomes; requires cprA as the mediator in CC electron donation from NADPH. CC -!- CATALYTIC ACTIVITY: Benzoate + NADPH + O(2) = 4-hydroxybenzoate + CC NADP(+) + H(2)O. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52521; CAA36753.1; -. DR EMBL; AJ347748; CAC69995.1; -. DR PIR; S12015; S12015. DR HSSP; P14779; 1JPZ. DR GO; GO:0005792; C:microsome; IDA. DR GO; GO:0018664; F:benzoate 4-monooxygenase activity; IDA. DR GO; GO:0006118; P:electron transport; IDA. DR InterPro; IPR001128; Cytochrome_P450. DR InterPro; IPR002401; EP450I. DR Pfam; PF00067; p450; 1. DR PIRSF; PIRSF000054; Pisatin_de-mtase; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. KW Electron transport; Heme; Monooxygenase; NADP; Oxidoreductase. FT METAL 461 461 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 517 AA; 58016 MW; 63FFBFDF703EC30B CRC64; MLALLLSPYG AYLGLALLVL YYLLPYLKRA HLRDIPAPGL AAFTNFWLLL QTRRGHRFVV VDNAHKKYGK LVRIAPRHTS IADDGAIQAV YGHGNGFLKS DFYDAFVSIH RGLFNTRDRA EHTRKRKTVS HTFSMKSIGQ FEQYIHGNIE LFVKQWNRMA DTQRNPKTGF ASLDALNWFN YLAFDIIGDL AFGAPFGMLD KGKDFAEMRK TPDSPPSYVQ AVEVLNRRGE VSATLGCYPA LKPFAKYLPD SFFRDGIQAV EDLAGIAVAR VNERLRPEVM ANNTRVDLLA RLMEGKDSNG EKLGRAELTA EALTQLIAGS DTTSNTSCAI LYWCMRTPGV IEKLHKALDE AIPQDVDVPT HAMVKDIPYL QWVIWETMRI HSTSAMGLPR EIPAGNPPVT ISGHTFYPGD VVSVPSYTIH RSKEIWGPDA EQFVPERWDP ARLTPRQKAA FIPFSTGPRA CVGRNVAEME LLVICGTVFR LFEFEMQQEG PMETREGFLR KPLGLQVGMK RRQPGSA //