FAP_CHLRE
ID FAP_CHLRE Reviewed; 611 AA.
AC A8JHB7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Fatty acid photodecarboxylase, chloroplastic {ECO:0000303|PubMed:28860382};
DE Short=CrFAP {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=CHLRE_12g514200v5 {ECO:0000312|EMBL:PNW75136.1},
GN CHLREDRAFT_140509 {ECO:0000312|EMBL:EDO96742.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RG Chlamydomonas Annotation Team;
RG JGI Annotation Team;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Grigoriev I.V., Rokhsar D.S.;
RT "WGS assembly of Chlamydomonas reinhardtii.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND 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 [4]
RP FUNCTION.
RX PubMed=30144559; DOI=10.1016/j.ymben.2018.08.008;
RA Yunus I.S., Wichmann J., Woerdenweber R., Lauersen K.J., Kruse O.,
RA Jones P.R.;
RT "Synthetic metabolic pathways for photobiological conversion of CO2 into
RT hydrocarbon fuel.";
RL Metab. Eng. 49:201-211(2018).
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:30144559). Substrate preference is toward fatty acids with C17
CC or C18 chains (PubMed:28860382, PubMed:30144559). Saturated fatty acids
CC are converted to alkanes, not alkenes (PubMed:28860382,
CC PubMed:30144559). The decarboxylation is initiated through electron
CC abstraction from the fatty acid by the photo-excited FAD (By
CC similarity). {ECO:0000250|UniProtKB:A0A248QE08,
CC ECO:0000269|PubMed:28860382, ECO:0000269|PubMed:30144559}.
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. {ECO:0000269|PubMed:28860382}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; DS496190; EDO96742.1; -; Genomic_DNA.
DR EMBL; CM008973; PNW75136.1; -; Genomic_DNA.
DR RefSeq; XP_001703004.1; XM_001702952.1.
DR AlphaFoldDB; A8JHB7; -.
DR SMR; A8JHB7; -.
DR STRING; 3055.EDO96742; -.
DR PaxDb; A8JHB7; -.
DR PRIDE; A8JHB7; -.
DR EnsemblPlants; PNW75136; PNW75136; CHLRE_12g514200v5.
DR GeneID; 5728543; -.
DR Gramene; PNW75136; PNW75136; CHLRE_12g514200v5.
DR KEGG; cre:CHLRE_12g514200v5; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_7_1_1; -.
DR InParanoid; A8JHB7; -.
DR OMA; GPESYAM; -.
DR OrthoDB; 798314at2759; -.
DR Proteomes; UP000006906; Chromosome 12.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008812; F:choline dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IBA:GO_Central.
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 Chloroplast; FAD; Flavoprotein; Lyase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..611
FT /note="Fatty acid photodecarboxylase, chloroplastic"
FT /id="PRO_0000450330"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55..56
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A248QE08"
FT BINDING 76
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A248QE08"
FT BINDING 125
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A248QE08"
FT BINDING 129
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A248QE08"
FT BINDING 133..136
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A248QE08"
FT BINDING 392
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:A0A248QE08"
FT BINDING 412
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:A0A248QE08"
FT BINDING 427
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:A0A248QE08"
FT BINDING 447
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000250|UniProtKB:A0A248QE08"
FT BINDING 582
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A0A248QE08"
SQ SEQUENCE 611 AA; 64459 MW; EEEB7D8BB26F21F0 CRC64;
MMLGPKTVTR GATKGAAPRS MAARRVGGAR RLSVRAAAGP AGSEKFDYVL VGGGTASCVL
ANKLSADGNK KVLVLEAGPT GDAMEVAVPA GITRLFAHPV MDWGMSSLTQ KQLVAREIYL
ARGRMLGGSS GSNATLYHRG SAADYDAWGL EGWSSKDVLD WFVKAECYAD GPKPYHGTGG
SMNTEQPRYE NVLHDEFFKA AAATGLPANP DFNDWSHPQD GFGEFQVSQK KGQRADTYRT
YLKPAMARGN LKVVIGARAT KVNIEKGSSG ARTTGVEYAM QQFGDRFTAE LAPGGEVLMC
SGAVHTPHLL MLSGVGPAAT LKEHGIDVVS DLSGVGQNLQ DHPAAVLAAR AKPEFEKLSV
TSEVYDDKCN IKLGAVAQYL FQRRGPLATT GCDHGAFVRT SSSLSQPDLQ MRFVPGCALD
PDGVKSYIVF GELKKQGRAW PGGITLQLLA IRAKSKGSIG LKAADPFINP AININYFSDP
ADLATLVNAV KMARKIAAQE PLKKYLQEET FPGERASSDK DLEEYIRRTV HSGNALVGTA
AMGASPAAGA VVSSADLKVF GVEGLRVVDA SVLPRIPGGQ TGAATVMVAE RAAALLRGQA
TIAPSRQPVA V
