TCMO_CICAR
ID TCMO_CICAR Reviewed; 505 AA.
AC O81928;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 99.
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=CYP73A19; Synonyms=CYP73;
OS Cicer arietinum (Chickpea) (Garbanzo).
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; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. ILC 3279;
RX PubMed=10773344; DOI=10.1016/s0168-9452(00)00214-4;
RA Overkamp S., Hein F., Barz W.;
RT "Cloning and characterization of eight cytochrome P450 cDNAs from chickpea
RT (Cicer arietinum L.) cell suspension cultures.";
RL Plant Sci. 155:101-108(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. ILC 3279;
RA Overkamp S., Barz W.;
RT "Isolation of a full length cDNA encoding trans-cinnamate 4-hydroxylase
RT from chickpea (Cicer arietinum L.).";
RL (er) Plant Gene Register PGR99-086(1999).
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 -!- DEVELOPMENTAL STAGE: Detectable 2 hours after elicitation and
CC disappears after 6 hours. {ECO:0000269|PubMed:10773344}.
CC -!- INDUCTION: By elicitation. {ECO:0000269|PubMed:10773344}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AJ007449; CAA07519.2; -; mRNA.
DR PIR; T09525; T09525.
DR RefSeq; NP_001266151.1; NM_001279222.1.
DR AlphaFoldDB; O81928; -.
DR SMR; O81928; -.
DR STRING; 3827.XP_004490717.1; -.
DR GeneID; 101492721; -.
DR KEGG; cam:101492721; -.
DR eggNOG; KOG0156; Eukaryota.
DR OrthoDB; 702827at2759; -.
DR UniPathway; UPA00825; UER00789.
DR Proteomes; UP000087171; Chromosome Ca2.
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; IEA:UniProtKB-EC.
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..505
FT /note="Trans-cinnamate 4-monooxygenase"
FT /id="PRO_0000052244"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 212..217
FT /ligand="(E)-cinnamate"
FT /ligand_id="ChEBI:CHEBI:15669"
FT /evidence="ECO:0000250|UniProtKB:Q94IP1"
FT BINDING 305
FT /ligand="(E)-cinnamate"
FT /ligand_id="ChEBI:CHEBI:15669"
FT /evidence="ECO:0000250|UniProtKB:Q94IP1"
FT BINDING 446
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 505 AA; 57889 MW; 453D1858FA996DC0 CRC64;
MDLLLLEKTL LALFIAATIA ITISKLRGKR FKLPPGPIPV PVFGNWLQVG DDLNHRNLTD
LAKRFGDIFL LRMGQRNLVV VSSPELAKEV LHTQGVEFGS RTRNVVFDIF TGKGQDMVFT
VYGTLAEMRR IMTVPFFTNK VVQQYRFGWE FEAQSVVDDV KKNPEACSSG IVLRRRLQLM
MYNIMYRIMF DRRFESEEDP LFVKLKALNG ERSRLAQSFE YNYGDFIPIL RPFLKGYLKL
CKEVKDRRLQ LFKDYFVDER KKLGSTKSTT NEGLKCAIDH ILDAQQKGEI NDDNVLYIVE
NINVAAIETT LWSIEWGIAE LVNHQKIQNK VREEIDRVLG PGHQVTEPDL QKLPYLQAVI
KETLRLRMAI PLLVPHMNLH DAKLSGFDIP AESKILVNAW WLANNPAQWK KPEEFRPERF
LEEESHVEAN GNDFRYLPFG VGRRSCPGII LALPILGITL GRLVQNFELL PPPGQSKIDT
AEKGGQFSLH ILKHSTIVCK PRSFN
