TCMO_SOYBN
ID TCMO_SOYBN Reviewed; 506 AA.
AC Q42797;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Trans-cinnamate 4-monooxygenase;
DE EC=1.14.14.91 {ECO:0000250|UniProtKB:Q04468};
DE AltName: Full=Cinnamic acid 4-hydroxylase;
DE Short=C4H;
DE Short=CA4H;
DE AltName: Full=Cytochrome P450 73;
DE AltName: Full=Cytochrome P450C4H;
GN Name=CYP73A11;
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Harosoy 63;
RX PubMed=9648734; DOI=10.1007/s004380050736;
RA Schopfer C.R., Ebel J.;
RT "Identification of elicitor-induced cytochrome P450s of soybean (Glycine
RT max L.) using differential display of mRNA.";
RL Mol. Gen. Genet. 258:315-322(1998).
CC -!- FUNCTION: Catalyzes the first oxidative step of the phenylpropanoid
CC pathway in higher plants by transforming trans-cinnamate into p-
CC coumarate (By similarity). The compounds formed by this pathway are
CC essential components for lignification, pollination, and defense
CC against ultraviolet light, predators and pathogens (By similarity).
CC {ECO:0000250|UniProtKB:Q04468}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamate + O2 + reduced [NADPH--hemoprotein reductase] =
CC (E)-4-coumarate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:10608, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:12876, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15669, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.91;
CC Evidence={ECO:0000250|UniProtKB:Q04468};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC -!- PATHWAY: Phenylpropanoid metabolism; trans-4-coumarate biosynthesis;
CC trans-4-coumarate from trans-cinnamate: step 1/1. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: By fungal elicitor.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; X92437; CAA63172.1; -; mRNA.
DR RefSeq; NP_001237317.1; NM_001250388.2.
DR AlphaFoldDB; Q42797; -.
DR SMR; Q42797; -.
DR STRING; 3847.GLYMA02G40290.1; -.
DR PRIDE; Q42797; -.
DR EnsemblPlants; KRH72830; KRH72830; GLYMA_02G236500.
DR GeneID; 100499623; -.
DR Gramene; KRH72830; KRH72830; GLYMA_02G236500.
DR KEGG; gmx:100499623; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q42797; -.
DR OMA; QIRLGNC; -.
DR OrthoDB; 702827at2759; -.
DR UniPathway; UPA00825; UER00789.
DR Proteomes; UP000008827; Chromosome 2.
DR Genevisible; Q42797; GM.
DR GO; GO:0016021; C:integral component of 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:0016710; F:trans-cinnamate 4-monooxygenase activity; IBA:GO_Central.
DR GO; GO:0009808; P:lignin 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 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..506
FT /note="Trans-cinnamate 4-monooxygenase"
FT /id="PRO_0000052254"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 213..218
FT /ligand="(E)-cinnamate"
FT /ligand_id="ChEBI:CHEBI:15669"
FT /evidence="ECO:0000250|UniProtKB:Q94IP1"
FT BINDING 307
FT /ligand="(E)-cinnamate"
FT /ligand_id="ChEBI:CHEBI:15669"
FT /evidence="ECO:0000250|UniProtKB:Q94IP1"
FT BINDING 448
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|UniProtKB:Q94IP1"
SQ SEQUENCE 506 AA; 58011 MW; 0BA3F890EEE4FE19 CRC64;
MDLLLLEKTL IGLFLAAVVA IAVSTLRGRK FKLPPGPLPV PIFGNWLQVG DDLNHRNLTD
LAKKFGDIFL LRMGQRNLVV VSSPELAKEV LHTQGVEFGS RTRNVVFDIF TGKGQDMVFT
VYGEHWRKMR RIMTVPFFTN KVVQQYRHGW ESEAAAVVED VKKNPDAAVS GTVIRRRLQL
MMYNNMYRIM FDRRFESEED PIFQRLRALN GERSRLAQSF EYNYGDFIPI LRPFLKGYLK
ICKEVKETRL KLFKDYFVDE RKKLGSTKST NNNNELKCAI DHILDAQRKG EINEDNVLYI
VENINVAAIE TTLWSIEWGI AELVNHPEIQ QKLRDEIDRV LGAGHQVTEP DIQKLPYLQA
VVKETLRLRM AIPLLVPHMN LHDAKLGGYD IPAESKILVN AWWLANNPAH WKKPEEFRPE
RFFEEESLVE ANGNDFRYLP FGVGRRSCPG IILALPILGI TLGRLVQNFE LLPPPGQSQI
DTSEKGGQFS LHILKHSTIV AKPRSF
