ID A0A0S3R2Z7_PHAAN Unreviewed; 520 AA.
AC A0A0S3R2Z7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN Name=Vigan.01G265200 {ECO:0000313|EMBL:BAT74879.1};
GN ORFNames=VIGAN_01265200 {ECO:0000313|EMBL:BAT74879.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT74879.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT74879.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP015034; BAT74879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3R2Z7; -.
DR Proteomes; UP000291084; Chromosome 1.
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; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd11075; CYP77_89; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24298:SF800; CYTOCHROME P450 89A2-RELATED; 1.
DR PANTHER; PTHR24298; FLAVONOID 3'-MONOOXYGENASE-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084}.
SQ SEQUENCE 520 AA; 60368 MW; 2DAB81EE727CBE8E CRC64;
MWCLLSGFDS SSSTQHRSDP LVKPLMEPCI FIILSLCFCV LIRRFFFSRR IKPTTPPGPS
HIPIISTILW LTKSFQIEPI LRTLHAKYGP ILTLHIATTP VVFVRDRFLA HQALVQNGSL
FSDRPKALAV AKIITTHQHN ISSASYGATW RTLRRNLTSQ MLHHSRVKSF SGIRTWVLHT
LLTHLKSQSQ SNNSVRVIDH FQYSMFCLLV FMCFGERLDD GKVRDIERVQ RQMLLRFRSF
DILNFWPRVT RVLLCKHWEE LLRLRKEQED VLVPLIRSRK QKQSKEEGVV SYVDTLLDLQ
LPEEKRKLNE EELVTLCNEF LNAGTDTTST ALQWIMANLV KYPHVQERVV DEIREVLGER
EEREVKEEEL QKLPYLKAVV LEGLRRHPPG HFVLPHSVTE DVVLNDYLVP KNTTVNFMVA
EMGWDPKVWE DPMAFKPERF MNDEFDITGS KEIKMMPFGA GRRICPGYNL ALLHLEYFVA
NLVSNFEWKV PEGGDVDLSE KQEFTVVMKN ALKVHLSPRI
//