GLO12_ORYSI
ID GLO12_ORYSI Reviewed; 628 AA.
AC B8AIW3;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Very-long-chain aldehyde decarbonylase GL1-2 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE AltName: Full=Protein GLOSSY 1-2 {ECO:0000305};
GN Name=GL1-2 {ECO:0000305}; ORFNames=OsI_06088 {ECO:0000312|EMBL:EEC72610.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Aldehyde decarbonylase involved in the conversion of
CC aldehydes to alkanes. Core component of a very-long-chain alkane
CC synthesis complex. {ECO:0000250|UniProtKB:F4HVY0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty aldehyde + H(+) + 2 NADPH + O2 = a long-
CC chain alkane + formate + H2O + 2 NADP(+); Xref=Rhea:RHEA:21440,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:17176, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:83563; EC=4.1.99.5;
CC Evidence={ECO:0000250|UniProtKB:F4HVY0};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:F4HVY0}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:F4HVY0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:F4HVY0}.
CC -!- SIMILARITY: Belongs to the sterol desaturase family. {ECO:0000305}.
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DR EMBL; CM000127; EEC72610.1; -; Genomic_DNA.
DR AlphaFoldDB; B8AIW3; -.
DR SMR; B8AIW3; -.
DR STRING; 39946.B8AIW3; -.
DR EnsemblPlants; BGIOSGA007025-TA; BGIOSGA007025-PA; BGIOSGA007025.
DR Gramene; BGIOSGA007025-TA; BGIOSGA007025-PA; BGIOSGA007025.
DR HOGENOM; CLU_017842_2_0_1; -.
DR OMA; PAQNCKT; -.
DR Proteomes; UP000007015; Chromosome 2.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:1990465; F:aldehyde oxygenase (deformylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0009924; F:octadecanal decarbonylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0046184; P:aldehyde biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0043447; P:alkane biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR GO; GO:0010025; P:wax biosynthetic process; IEA:EnsemblPlants.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR021940; Uncharacterised_Wax2_C.
DR Pfam; PF04116; FA_hydroxylase; 1.
DR Pfam; PF12076; Wax2_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Lyase; Membrane; NADP; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..628
FT /note="Very-long-chain aldehyde decarbonylase GL1-2"
FT /id="PRO_0000445871"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 137..277
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
SQ SEQUENCE 628 AA; 71028 MW; 3A90727CB83E420A CRC64;
MAAPPLSSWP WASLGSYKYV LYGAVVWKVA EEWRQQGAAP VGSWWLHLLL LFAARGLTYQ
FWFSYGNMLF FTRRRRVVPD SVDFRQVDAE WDWDNFLLLQ TLIGATLVGS PAVARQQLLL
PSLKQAWDPR GWAIALLLHV LVAEPLFYWA HRALHRAPLF SRYHAAHHHA SVTTPLTAGF
GTPLESLLLT VVIGVPLAGA FLMGVGSVGL VYGHVLLFDF LRSMGYSNVE VISPRVFQAV
PLLRYLIYTP TYLSLHHREK DSNFCLFMPI FDLLGGTLNH KSWELQKEVY LGKNDQAPDF
VFLAHVVDIM ASMHVPFVLR SCSSTPFANH FVLLPFWPVA FGFMLLMWCC SKNFLVSSYR
LRGNLHQMWT VPRYGFQYFI PAAKKGINEQ IELAILRADR MGVKVLSLAA LNKNEALNGG
GTLFVNKHPE LRVRVVHGNT LTAAVILNEI PSNVKDVFLT GATSKLGRAI ALYLCRKKIR
VLMLTLSSER FLKIQREAPA EFQQYLVQVT KYQPAQNCKT WLVGKWLSPR EQRWAPAGTH
FHQFVVPPII GFRRDCTYGK LAAMRLPKDV QGLGYCEYTM ERGVVHACHA GGVVHFLEGW
EHHEVGAIDV DRIDVVWKAA LKHGLTPA
