CP120_SYNY3
ID CP120_SYNY3 Reviewed; 444 AA.
AC Q59990;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Putative cytochrome P450 120;
DE EC=1.14.-.-;
GN Name=cyp120; Synonyms=cyp; OrderedLocusNames=slr0574;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; BA000022; BAA10496.1; -; Genomic_DNA.
DR PIR; S75761; S75761.
DR PDB; 2VE3; X-ray; 2.10 A; A/B=1-444.
DR PDB; 2VE4; X-ray; 2.40 A; A/B=1-444.
DR PDBsum; 2VE3; -.
DR PDBsum; 2VE4; -.
DR AlphaFoldDB; Q59990; -.
DR SMR; Q59990; -.
DR STRING; 1148.1001252; -.
DR PaxDb; Q59990; -.
DR EnsemblBacteria; BAA10496; BAA10496; BAA10496.
DR KEGG; syn:slr0574; -.
DR eggNOG; COG2124; Bacteria.
DR InParanoid; Q59990; -.
DR OMA; AHMCLGL; -.
DR PhylomeDB; Q59990; -.
DR EvolutionaryTrace; Q59990; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..444
FT /note="Putative cytochrome P450 120"
FT /id="PRO_0000052272"
FT BINDING 391
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:0000250"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:2VE3"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:2VE3"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:2VE3"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2VE3"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 121..137
FT /evidence="ECO:0007829|PDB:2VE3"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 143..159
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:2VE3"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 192..215
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 241..272
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 274..285
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 302..314
FT /evidence="ECO:0007829|PDB:2VE3"
FT STRAND 320..327
FT /evidence="ECO:0007829|PDB:2VE3"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:2VE3"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:2VE3"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:2VE3"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:2VE3"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:2VE3"
FT TURN 372..375
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:2VE3"
FT HELIX 394..411
FT /evidence="ECO:0007829|PDB:2VE3"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:2VE3"
FT STRAND 424..432
FT /evidence="ECO:0007829|PDB:2VE3"
FT STRAND 437..442
FT /evidence="ECO:0007829|PDB:2VE3"
SQ SEQUENCE 444 AA; 50578 MW; 8F62A9EED3B54BDC CRC64;
MITSPTNLNS LPIPPGDFGL PWLGETLNFL NDGDFGKKRQ QQFGPIFKTR LFGKNVIFIS
GALANRFLFT KEQETFQATW PLSTRILLGP NALATQMGEI HRSRRKILYQ AFLPRTLDSY
LPKMDGIVQG YLEQWGKANE VIWYPQLRRM TFDVAATLFM GEKVSQNPQL FPWFETYIQG
LFSLPIPLPN TLFGKSQRAR ALLLAELEKI IKARQQQPPS EEDALGILLA ARDDNNQPLS
LPELKDQILL LLFAGHETLT SALSSFCLLL GQHSDIRERV RQEQNKLQLS QELTAETLKK
MPYLDQVLQE VLRLIPPVGG GFRELIQDCQ FQGFHFPKGW LVSYQISQTH ADPDLYPDPE
KFDPERFTPD GSATHNPPFA HVPFGGGLRE CLGKEFARLE MKLFATRLIQ QFDWTLLPGQ
NLELVVTPSP RPKDNLRVKL HSLM
