CYPA2_RHOPA
ID CYPA2_RHOPA Reviewed; 412 AA.
AC Q6N8N2;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cytochrome p450 CYP199A2 {ECO:0000303|PubMed:16472768};
DE EC=1.14.99.15 {ECO:0000269|PubMed:16472768, ECO:0000269|PubMed:18762195};
DE AltName: Full=4-methoxybenzoate O-demethylase CYP199A2 {ECO:0000305};
DE AltName: Full=4-methoxybenzoate monooxygenase (O-demethylating) {ECO:0000305};
GN Name=cyp199a2 {ECO:0000303|PubMed:16472768};
GN OrderedLocusNames=RPA1871 {ECO:0000312|EMBL:CAE27312.1};
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND COFACTOR.
RC STRAIN=ATCC BAA-98 / CGA009 {ECO:0000303|PubMed:16472768};
RX PubMed=16472768; DOI=10.1016/j.bbrc.2006.01.133;
RA Bell S.G., Hoskins N., Xu F., Caprotti D., Rao Z., Wong L.L.;
RT "Cytochrome P450 enzymes from the metabolically diverse bacterium
RT Rhodopseudomonas palustris.";
RL Biochem. Biophys. Res. Commun. 342:191-196(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH HEME, FUNCTION,
RP CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=ATCC BAA-98 / CGA009 {ECO:0000303|PubMed:18762195};
RX PubMed=18762195; DOI=10.1016/j.jmb.2008.08.033;
RA Bell S.G., Xu F., Forward I., Bartlam M., Rao Z., Wong L.L.;
RT "Crystal structure of CYP199A2, a para-substituted benzoic acid oxidizing
RT cytochrome P450 from Rhodopseudomonas palustris.";
RL J. Mol. Biol. 383:561-574(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH HEME AND
RP 4-METHOXYBENZOATE, AND COFACTOR.
RC STRAIN=ATCC BAA-98 / CGA009 {ECO:0000303|PubMed:22695988};
RX PubMed=22695988; DOI=10.1039/c2dt30783a;
RA Bell S.G., Yang W., Tan A.B., Zhou R., Johnson E.O., Zhang A., Zhou W.,
RA Rao Z., Wong L.L.;
RT "The crystal structures of 4-methoxybenzoate bound CYP199A2 and CYP199A4:
RT structural changes on substrate binding and the identification of an anion
RT binding site.";
RL Dalton Trans. 41:8703-8714(2012).
CC -!- FUNCTION: The oxidative demethylation of 4-methoxybenzoate requires the
CC participation of the monooxygenase CYP199A2, the ferredoxin-like
CC protein ThcC/RPA1872 and a ferredoxin reductase to mediate the transfer
CC of electrons from NADH to CYP199A2. It is also active with 4-
CC ethylbenzoate. {ECO:0000269|PubMed:16472768,
CC ECO:0000269|PubMed:18762195}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methoxybenzoate + AH2 + O2 = 4-hydroxybenzoate + A +
CC formaldehyde + H2O; Xref=Rhea:RHEA:18613, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16639,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:17499, ChEBI:CHEBI:17879;
CC EC=1.14.99.15; Evidence={ECO:0000269|PubMed:16472768,
CC ECO:0000269|PubMed:18762195};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:16472768, ECO:0000269|PubMed:18762195,
CC ECO:0000269|PubMed:22695988};
CC -!- SUBUNIT: Interacts with the ferredoxin-like iron-sulfur protein ThcC.
CC {ECO:0000303|PubMed:16472768}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR EMBL; BX572599; CAE27312.1; -; Genomic_DNA.
DR RefSeq; WP_011157377.1; NC_005296.1.
DR PDB; 2FR7; X-ray; 2.01 A; A=1-412.
DR PDB; 4DNJ; X-ray; 1.80 A; A=1-412.
DR PDBsum; 2FR7; -.
DR PDBsum; 4DNJ; -.
DR AlphaFoldDB; Q6N8N2; -.
DR SMR; Q6N8N2; -.
DR STRING; 258594.RPA1871; -.
DR PRIDE; Q6N8N2; -.
DR EnsemblBacteria; CAE27312; CAE27312; RPA1871.
DR GeneID; 66892909; -.
DR KEGG; rpa:RPA1871; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_0_2_5; -.
DR OMA; RPELWPN; -.
DR PhylomeDB; Q6N8N2; -.
DR BioCyc; RPAL258594:TX73_RS09560-MON; -.
DR BRENDA; 1.14.99.15; 5412.
DR EvolutionaryTrace; Q6N8N2; -.
DR Proteomes; UP000001426; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0018690; F:4-methoxybenzoate monooxygenase (O-demethylating) activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..412
FT /note="Cytochrome p450 CYP199A2"
FT /id="PRO_0000430673"
FT BINDING 94..97
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22695988"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22695988"
FT BINDING 361
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:18762195,
FT ECO:0000269|PubMed:22695988"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:4DNJ"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4DNJ"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:4DNJ"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:4DNJ"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:4DNJ"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:4DNJ"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:4DNJ"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:4DNJ"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 120..143
FT /evidence="ECO:0007829|PDB:4DNJ"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:4DNJ"
FT TURN 230..234
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 254..269
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 284..295
FT /evidence="ECO:0007829|PDB:4DNJ"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:4DNJ"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4DNJ"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:4DNJ"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:4DNJ"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:4DNJ"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:4DNJ"
FT HELIX 364..381
FT /evidence="ECO:0007829|PDB:4DNJ"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:4DNJ"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:4DNJ"
FT STRAND 397..404
FT /evidence="ECO:0007829|PDB:4DNJ"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:4DNJ"
SQ SEQUENCE 412 AA; 44623 MW; 71E0DEA6E28EA89B CRC64;
MTTAPSLVPV TTPSQHGAGV PHLGIDPFAL DYFADPYPEQ ETLREAGPVV YLDKWNVYGV
ARYAEVYAVL NDPLTFCSSR GVGLSDFKKE KPWRPPSLIL EADPPAHTRT RAVLSKVLSP
ATMKRLRDGF AAAADAKIDE LLARGGNIDA IADLAEAYPL SVFPDAMGLK QEGRENLLPY
AGLVFNAFGP PNELRQSAIE RSAPHQAYVA EQCQRPNLAP GGFGACIHAF SDTGEITPEE
APLLVRSLLS AGLDTTVNGI AAAVYCLARF PDEFARLRAD PSLARNAFEE AVRFESPVQT
FFRTTTRDVE LAGATIGEGE KVLMFLGSAN RDPRRWDDPD RYDITRKTSG HVGFGSGVHM
CVGQLVARLE GEVVLAALAR KVAAIEIAGP LKRRFNNTLR GLESLPIQLT PA
