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Database: UniProt
Entry: A0A0K9NVJ5_ZOSMR
LinkDB: A0A0K9NVJ5_ZOSMR
Original site: A0A0K9NVJ5_ZOSMR 
ID   A0A0K9NVJ5_ZOSMR        Unreviewed;       530 AA.
AC   A0A0K9NVJ5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Cytochrome P450 90A1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ZOSMA_56G00100 {ECO:0000313|EMBL:KMZ60779.1};
OS   Zostera marina (Eelgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX   NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ60779.1, ECO:0000313|Proteomes:UP000036987};
RN   [1] {ECO:0000313|Proteomes:UP000036987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX   PubMed=26814964; DOI=10.1038/nature16548;
RA   Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA   Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA   Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA   Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA   Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA   Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA   Van de Peer Y.;
RT   "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT   the sea.";
RL   Nature 530:331-335(2016).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR602403-1};
CC   -!- PATHWAY: Hormone biosynthesis. {ECO:0000256|ARBA:ARBA00004972}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMZ60779.1}.
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DR   EMBL; LFYR01001565; KMZ60779.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K9NVJ5; -.
DR   STRING; 29655.A0A0K9NVJ5; -.
DR   OMA; KLWEVYM; -.
DR   OrthoDB; 758626at2759; -.
DR   Proteomes; UP000036987; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0016132; P:brassinosteroid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0010268; P:brassinosteroid homeostasis; IBA:GO_Central.
DR   GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR   CDD; cd11043; CYP90-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR   PANTHER; PTHR24286:SF44; CYTOCHROME P450 90A1; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602403-1};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         476
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:0000256|PIRSR:PIRSR602403-1"
SQ   SEQUENCE   530 AA;  60770 MW;  50E0BA4DE153BBD2 CRC64;
     MHPPPRSPLS YLLSVFMWSG VRWPVAGGTM KNWMSTLAFE PLMLLVLLIL PVTVLWFAWK
     RSRSSLPPGK QGFPLVGETM QLISAYRSEH PNSFMDERME MHGQVFTSHV FGETTVFSSD
     PDVNRHVLQK EGRLFQSSYP SSIGALLGKN SVVISRGPYH KQLHSFTLAS FSNQTVLRDL
     LLPDIDRLIR QNTIDAWKDG QTVILHEQAK KMTFEIAVKQ LMSREPGEWT EGLRRDYGLV
     IDGFFSIPFP FARLLPFTIY GRAIRARLRI AQQIRPVVTK RIRDFASGVR SEVVDVLDKL
     LMEEGVKDED KVVDYVFSML VGIHETTSIS MTCVVKFLTE NPAAMAELRE EHDKIKNKQE
     GSGFHWNDYK NMMPFTQCVI TETLRMSNIV SGVFRRCATD VDIKGFKIPK GRKIYASFRA
     VHMNEDYFED ARTFNPWRWM KKVDEDETEE DSKKKTATES DKKRLLCLFG GGPRLCPGYE
     LSRLELCVFL HYLVTSFTWD TAGEDSMVFF PTTRTVKGLP IRVSRRASCK
//
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