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GLO19_ORYSI
ID   GLO19_ORYSI             Reviewed;         258 AA.
AC   B8B4W4;
DT   05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Very-long-chain aldehyde decarbonylase GL1-9 {ECO:0000305};
DE            EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE   AltName: Full=Protein GLOSSY 1-9 {ECO:0000305};
GN   Name=GL1-9 {ECO:0000305}; ORFNames=OsI_26956 {ECO:0000312|EMBL:EEC82496.1};
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; CM000132; EEC82496.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8B4W4; -.
DR   STRING; 39946.B8B4W4; -.
DR   EnsemblPlants; BGIOSGA023874-TA; BGIOSGA023874-PA; BGIOSGA023874.
DR   Gramene; BGIOSGA023874-TA; BGIOSGA023874-PA; BGIOSGA023874.
DR   HOGENOM; CLU_043293_1_0_1; -.
DR   OMA; HMAYDLL; -.
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..258
FT                   /note="Very-long-chain aldehyde decarbonylase GL1-9"
FT                   /id="PRO_0000445883"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          101..237
FT                   /note="Fatty acid hydroxylase"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   258 AA;  29905 MW;  867A226FF9E086B3 CRC64;
     MVPWEGYVSD ETMGTFAPIA LYWVYAGGYQ LVLHRRPLER YRLHTRAEEE EKNLVALPAV
     VRGVLLQQLV QAIVAMILFM VTSDSSAVVV QPPIIIQAFQ FLVAMLVMDS WQYFVHRYMH
     QNKFLYRHIH SQHHRLIVPY AIGALYNHPL EGLLLDTVGG AISFLVSGMT PRTSVFFFCF
     AVLKTVDDHC GLWLPYNIFQ SLFQNNTAYH DVHHQLQGSK YNYSQPFFSI WDRILGTHMP
     YNLVRRKEGG FEARPLRD
 
 
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