FAP_CHLVA
ID FAP_CHLVA Reviewed; 654 AA.
AC A0A248QE08; A0A2D0TC92; E1ZTE9;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Fatty acid photodecarboxylase, chloroplastic {ECO:0000303|PubMed:28860382};
DE Short=CvFAP {ECO:0000303|PubMed:28860382};
DE EC=4.1.1.106 {ECO:0000269|PubMed:28860382};
DE Flags: Precursor;
GN Name=FAP {ECO:0000303|PubMed:28860382};
GN ORFNames=CHLNCDRAFT_28598 {ECO:0000312|EMBL:EFN50890.1};
OS Chlorella variabilis (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=554065;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) OF
RP 62-654 IN COMPLEX WITH FAD AND PALMITATE, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP BIOTECHNOLOGY.
RC STRAIN=NC64A;
RX PubMed=28860382; DOI=10.1126/science.aan6349;
RA Sorigue D., Legeret B., Cuine S., Blangy S., Moulin S., Billon E.,
RA Richaud P., Brugiere S., Coute Y., Nurizzo D., Mueller P., Brettel K.,
RA Pignol D., Arnoux P., Li-Beisson Y., Peltier G., Beisson F.;
RT "An algal photoenzyme converts fatty acids to hydrocarbons.";
RL Science 357:903-907(2017).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NC64A;
RX PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT "The Chlorella variabilis NC64A genome reveals adaptation to
RT photosymbiosis, coevolution with viruses, and cryptic sex.";
RL Plant Cell 22:2943-2955(2010).
RN [3]
RP FUNCTION.
RX PubMed=30106504; DOI=10.1002/anie.201807119;
RA Huijbers M.M.E., Zhang W., Tonin F., Hollmann F.;
RT "Light-driven enzymatic decarboxylation of fatty acids.";
RL Angew. Chem. Int. Ed. 57:13648-13651(2018).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=31462926; DOI=10.1186/s13068-019-1542-4;
RA Bruder S., Moldenhauer E.J., Lemke R.D., Ledesma-Amaro R., Kabisch J.;
RT "Drop-in biofuel production using fatty acid photodecarboxylase from
RT Chlorella variabilis in the oleaginous yeast Yarrowia lipolytica.";
RL Biotechnol. Biofuels 12:202-202(2019).
RN [5]
RP FUNCTION.
RX PubMed=30673222; DOI=10.1021/jacs.8b12282;
RA Zhang W., Ma M., Huijbers M.M.E., Filonenko G.A., Pidko E.A., van Schie M.,
RA de Boer S., Burek B.O., Bloh J.Z., van Berkel W.J.H., Smith W.A.,
RA Hollmann F.;
RT "Hydrocarbon synthesis via photoenzymatic decarboxylation of carboxylic
RT acids.";
RL J. Am. Chem. Soc. 141:3116-3120(2019).
CC -!- FUNCTION: Catalyzes the decarboxylation of free fatty acids to n-
CC alkanes or n-alkenes in response to blue light (PubMed:28860382,
CC PubMed:30106504, PubMed:30673222). Substrate preference is toward fatty
CC acids with C16 or C17 chains (PubMed:28860382, PubMed:30106504,
CC PubMed:30673222). Saturated fatty acids are converted to alkanes, not
CC alkenes (PubMed:28860382). The decarboxylation is initiated through
CC electron abstraction from the fatty acid by the photo-excited FAD
CC (PubMed:28860382). {ECO:0000269|PubMed:28860382,
CC ECO:0000269|PubMed:30106504, ECO:0000269|PubMed:30673222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + H(+) + hnu = a long-chain alkane +
CC CO2; Xref=Rhea:RHEA:18969, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30212, ChEBI:CHEBI:57560, ChEBI:CHEBI:83563;
CC EC=4.1.1.106; Evidence={ECO:0000269|PubMed:28860382};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18970;
CC Evidence={ECO:0000269|PubMed:28860382};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoate + hnu = CO2 + pentadecane;
CC Xref=Rhea:RHEA:56060, ChEBI:CHEBI:7896, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:28897, ChEBI:CHEBI:30212;
CC EC=4.1.1.106; Evidence={ECO:0000269|PubMed:28860382};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56061;
CC Evidence={ECO:0000269|PubMed:28860382};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:28860382};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:28860382};
CC -!- ACTIVITY REGULATION: Activated by blue light and repressed by red
CC light. {ECO:0000269|PubMed:28860382}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5 (with palmitate as substrate).
CC {ECO:0000269|PubMed:28860382};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- BIOTECHNOLOGY: May be used in light-driven, bio-based production of
CC hydrocarbons (PubMed:28860382). The oleaginous yeast Yarrowia
CC lipolytica expressing FAP from Chlorella variabilis under blue light
CC conditions produces odd-numbered alkanes and alkenes, which could be
CC used as drop-in biofuel (PubMed:31462926).
CC {ECO:0000269|PubMed:28860382, ECO:0000269|PubMed:31462926}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EFN50890.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KY511411; ASM79489.1; -; mRNA.
DR EMBL; GL433871; EFN50890.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_005842992.1; XM_005842930.1.
DR PDB; 5NCC; X-ray; 3.12 A; A/B/C/D/E/F=62-654.
DR PDB; 6YRU; X-ray; 1.78 A; AAA=77-654.
DR PDB; 6YRV; X-ray; 1.94 A; AAA=77-654.
DR PDB; 6YRX; X-ray; 1.87 A; AAA=77-654.
DR PDB; 6YRZ; X-ray; 1.82 A; AAA=77-654.
DR PDB; 6YS1; X-ray; 1.64 A; AAA=77-654.
DR PDB; 6YS2; X-ray; 1.97 A; AAA=77-654.
DR PDB; 6ZH7; X-ray; 2.00 A; A/B=76-654.
DR PDB; 7AV4; X-ray; 1.94 A; AAA=1-654.
DR PDBsum; 5NCC; -.
DR PDBsum; 6YRU; -.
DR PDBsum; 6YRV; -.
DR PDBsum; 6YRX; -.
DR PDBsum; 6YRZ; -.
DR PDBsum; 6YS1; -.
DR PDBsum; 6YS2; -.
DR PDBsum; 6ZH7; -.
DR PDBsum; 7AV4; -.
DR AlphaFoldDB; A0A248QE08; -.
DR SMR; A0A248QE08; -.
DR STRING; 554065.XP_005842992.1; -.
DR GeneID; 17350319; -.
DR KEGG; cvr:CHLNCDRAFT_28598; -.
DR eggNOG; KOG1238; Eukaryota.
DR OrthoDB; 798314at2759; -.
DR Proteomes; UP000008141; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; FAD; Flavoprotein; Lyase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..654
FT /note="Fatty acid photodecarboxylase, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000450329"
FT BINDING 93..94
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28860382,
FT ECO:0007744|PDB:5NCC"
FT BINDING 114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28860382,
FT ECO:0007744|PDB:5NCC"
FT BINDING 162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28860382,
FT ECO:0007744|PDB:5NCC"
FT BINDING 166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28860382,
FT ECO:0007744|PDB:5NCC"
FT BINDING 170..173
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28860382,
FT ECO:0007744|PDB:5NCC"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28860382,
FT ECO:0007744|PDB:5NCC"
FT BINDING 432
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:28860382,
FT ECO:0007744|PDB:5NCC"
FT BINDING 451
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:28860382,
FT ECO:0007744|PDB:5NCC"
FT BINDING 466
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:28860382,
FT ECO:0007744|PDB:5NCC"
FT BINDING 486
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:28860382,
FT ECO:0007744|PDB:5NCC"
FT BINDING 622
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:28860382,
FT ECO:0007744|PDB:5NCC"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:5NCC"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:5NCC"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 192..202
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 230..242
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 276..280
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 297..304
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 311..321
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 328..339
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 342..352
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 358..363
FT /evidence="ECO:0007829|PDB:6ZH7"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 383..391
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:5NCC"
FT HELIX 400..404
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 413..422
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 448..455
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 458..461
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 462..471
FT /evidence="ECO:0007829|PDB:6ZH7"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 482..491
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 510..512
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 522..539
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 541..544
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 560..570
FT /evidence="ECO:0007829|PDB:6ZH7"
FT STRAND 603..607
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:6ZH7"
FT HELIX 622..636
FT /evidence="ECO:0007829|PDB:6ZH7"
SQ SEQUENCE 654 AA; 68824 MW; 0CC56D0FA3D1B4DA CRC64;
MASITSRASA RASCSQANTR AGRVALSGGA LLRPARPARS FVPARKQQQG AVRRGGALSA
RASAVEDIRK VLSDSSSPVA GQKYDYILVG GGTAACVLAN RLSADGSKRV LVLEAGPDNT
SRDVKIPAAI TRLFRSPLDW NLFSELQEQL AERQIYMARG RLLGGSSATN ATLYHRGAAG
DYDAWGVEGW SSEDVLSWFV QAETNADFGP GAYHGSGGPM RVENPRYTNK QLHTAFFKAA
EEVGLTPNSD FNDWSHDHAG YGTFQVMQDK GTRADMYRQY LKPVLGRRNL QVLTGAAVTK
VNIDQAAGKA QALGVEFSTD GPTGERLSAE LAPGGEVIMC AGAVHTPFLL KHSGVGPSAE
LKEFGIPVVS NLAGVGQNLQ DQPACLTAAP VKEKYDGIAI SDHIYNEKGQ IRKRAIASYL
LGGRGGLTST GCDRGAFVRT AGQALPDLQV RFVPGMALDP DGVSTYVRFA KFQSQGLKWP
SGITMQLIAC RPQSTGSVGL KSADPFAPPK LSPGYLTDKD GADLATLRKG IHWARDVARS
SALSEYLDGE LFPGSGVVSD DQIDEYIRRS IHSSNAITGT CKMGNAGDSS SVVDNQLRVH
GVEGLRVVDA SVVPKIPGGQ TGAPVVMIAE RAAALLTGKA TIGASAAAPA TVAA
