CRTI_PANAN
ID CRTI_PANAN Reviewed; 492 AA.
AC P21685;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Phytoene desaturase (lycopene-forming);
DE EC=1.3.99.31;
DE AltName: Full=4-step phytoene desaturase;
DE AltName: Full=Phytoene dehydrogenase;
GN Name=crtI;
OS Pantoea ananas (Erwinia uredovora).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=553;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=ATCC 19321 / DSM 30080 / NCPPB 800 / NRRL B-14773 / 20D3;
RX PubMed=2254247; DOI=10.1128/jb.172.12.6704-6712.1990;
RA Misawa N., Nakagawa M., Kobayashi K., Yamano S., Izawa Y., Nakamura K.,
RA Harashima K.;
RT "Elucidation of the Erwinia uredovora carotenoid biosynthetic pathway by
RT functional analysis of gene products expressed in Escherichia coli.";
RL J. Bacteriol. 172:6704-6712(1990).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, PATHWAY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=1400305; DOI=10.1016/s0021-9258(19)88639-8;
RA Fraser P.D., Misawa N., Linden H., Yamano S., Kobayashi K., Sandmann G.;
RT "Expression in Escherichia coli, purification, and reactivation of the
RT recombinant Erwinia uredovora phytoene desaturase.";
RL J. Biol. Chem. 267:19891-19895(1992).
CC -!- FUNCTION: Converts 15-cis-phytoene into all-trans-lycopene via the
CC intermediary of all-trans-phytofluene, all-trans-zeta-carotene and all-
CC trans-neurosporene, by the introduction of four double bonds.
CC {ECO:0000269|PubMed:1400305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15-cis-phytoene + 4 A = 4 AH2 + all-trans-lycopene;
CC Xref=Rhea:RHEA:15585, ChEBI:CHEBI:13193, ChEBI:CHEBI:15948,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:27787; EC=1.3.99.31;
CC Evidence={ECO:0000269|PubMed:1400305};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:1400305};
CC -!- ACTIVITY REGULATION: Inhibited by NAD and NADP.
CC {ECO:0000269|PubMed:1400305}.
CC -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC {ECO:0000269|PubMed:1400305, ECO:0000269|PubMed:2254247}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1400305}.
CC -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; D90087; BAA14127.1; -; Genomic_DNA.
DR PIR; D37802; D37802.
DR PDB; 4DGK; X-ray; 2.35 A; A=1-492.
DR PDBsum; 4DGK; -.
DR AlphaFoldDB; P21685; -.
DR SMR; P21685; -.
DR PRIDE; P21685; -.
DR BioCyc; MetaCyc:MON-15564; -.
DR BRENDA; 1.3.99.31; 2137.
DR UniPathway; UPA00803; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IDA:UniProtKB.
DR GO; GO:0016120; P:carotene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 3.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR014105; Carotenoid/retinoid_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR008150; Phytoene_DH_bac_CS.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02734; crtI_fam; 1.
DR PROSITE; PS00982; PHYTOENE_DH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carotenoid biosynthesis; Cell membrane; FAD; Flavoprotein;
KW Membrane; Oxidoreductase.
FT CHAIN 1..492
FT /note="Phytoene desaturase (lycopene-forming)"
FT /id="PRO_0000067686"
FT BINDING 5..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:4DGK"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 80..91
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 117..131
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4DGK"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 177..191
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 305..315
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 368..376
FT /evidence="ECO:0007829|PDB:4DGK"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 386..404
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:4DGK"
FT TURN 421..424
FT /evidence="ECO:0007829|PDB:4DGK"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:4DGK"
FT HELIX 472..491
FT /evidence="ECO:0007829|PDB:4DGK"
SQ SEQUENCE 492 AA; 55008 MW; FA4CD4E34A9C6413 CRC64;
MKPTTVIGAG FGGLALAIRL QAAGIPVLLL EQRDKPGGRA YVYEDQGFTF DAGPTVITDP
SAIEELFALA GKQLKEYVEL LPVTPFYRLC WESGKVFNYD NDQTRLEAQI QQFNPRDVEG
YRQFLDYSRA VFKEGYLKLG TVPFLSFRDM LRAAPQLAKL QAWRSVYSKV ASYIEDEHLR
QAFSFHSLLV GGNPFATSSI YTLIHALERE WGVWFPRGGT GALVQGMIKL FQDLGGEVVL
NARVSHMETT GNKIEAVHLE DGRRFLTQAV ASNADVVHTY RDLLSQHPAA VKQSNKLQTK
RMSNSLFVLY FGLNHHHDQL AHHTVCFGPR YRELIDEIFN HDGLAEDFSL YLHAPCVTDS
SLAPEGCGSY YVLAPVPHLG TANLDWTVEG PKLRDRIFAY LEQHYMPGLR SQLVTHRMFT
PFDFRDQLNA YHGSAFSVEP VLTQSAWFRP HNRDKTITNL YLVGAGTHPG AGIPGVIGSA
KATAGLMLED LI
