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Database: UniProt
Entry: A0A0S3R2Z7_PHAAN
LinkDB: A0A0S3R2Z7_PHAAN
Original site: A0A0S3R2Z7_PHAAN 
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}.
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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
//
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