GLO18_ORYSI
ID GLO18_ORYSI Reviewed; 268 AA.
AC B8B6I2;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2018, sequence version 2.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Very-long-chain aldehyde decarbonylase GL1-8 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE AltName: Full=Protein GLOSSY 1-8 {ECO:0000305};
GN Name=GL18 {ECO:0000305}; ORFNames=OsI_24570 {ECO:0000312|EMBL:EEC81368.1};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEC81368.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CM000132; EEC81368.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; B8B6I2; -.
DR SMR; B8B6I2; -.
DR STRING; 39946.B8B6I2; -.
DR EnsemblPlants; BGIOSGA024996-TA; BGIOSGA024996-PA; BGIOSGA024996.
DR Gramene; BGIOSGA024996-TA; BGIOSGA024996-PA; BGIOSGA024996.
DR HOGENOM; CLU_047036_5_3_1; -.
DR Proteomes; UP000007015; Chromosome 7.
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:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR GO; GO:1901700; P:response to oxygen-containing compound; IEA:UniProt.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR Pfam; PF04116; FA_hydroxylase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Lyase; Membrane; NADP; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..268
FT /note="Very-long-chain aldehyde decarbonylase GL1-8"
FT /id="PRO_0000445881"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 114..249
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
SQ SEQUENCE 268 AA; 31298 MW; 523B389FD2174146 CRC64;
MMAAAGLESA WEYLITHFSE FQLASIGTFL LHESVFFLSG LPSLLFERLG LFSKYKIQKK
SNTPDYQNRC VVRLVLYHVC VNLPLTILSY RTFKFMGLRS TLPLPHWTVV VSQVLFFFVL
EDFIFYWGHR ALHTKWLYQH VHSVHHEYAT PFGLTSEYAH PAEILFLGFA TVAGPALTGP
HLFTLWVWMV LRVLETVEAH SGYHFPWSPS NFLPLYGGAE FHDYHHRVLY TKSGNYSSTF
IYMDWLFGTD KDYRKTKALE EKERTKHL
