GLO16_ORYSI
ID GLO16_ORYSI Reviewed; 635 AA.
AC A2XAY1;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Very-long-chain aldehyde decarbonylase GL1-6 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE AltName: Full=Protein GLOSSY 1-6 {ECO:0000305};
GN Name=GL1-6 {ECO:0000305}; ORFNames=OsI_09413 {ECO:0000312|EMBL:EAY87991.1};
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; EAY87991.1; -; Genomic_DNA.
DR AlphaFoldDB; A2XAY1; -.
DR STRING; 39946.A2XAY1; -.
DR EnsemblPlants; BGIOSGA005375-TA; BGIOSGA005375-PA; BGIOSGA005375.
DR Gramene; BGIOSGA005375-TA; BGIOSGA005375-PA; BGIOSGA005375.
DR HOGENOM; CLU_017842_1_0_1; -.
DR OMA; VCENWLP; -.
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:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
DR GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
DR GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR InterPro; IPR006694; Fatty_acid_hydroxylase.
DR InterPro; IPR021940; Uncharacterised_Wax2_C.
DR Pfam; PF04116; FA_hydroxylase; 1.
DR Pfam; PF12076; Wax2_C; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Lyase; Membrane; NADP; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..635
FT /note="Very-long-chain aldehyde decarbonylase GL1-6"
FT /id="PRO_0000445878"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 139..273
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
SQ SEQUENCE 635 AA; 71639 MW; C7464F39B0B9BA7B CRC64;
MASKPGPLTQ WPWNNLGNYK YALVAPSAAY STYRFVTASS AAERDLLNFM VFPMLLLRLL
YGQLWITVSR HQTARSKHKI VNKSLDFEQI DRERNWDDQI ILTALVFYLV SATMPQAQVA
PWWSTKGMVV TAVLHAGPVE FLYYWLHRAL HHHWLYARYH SHHHASIVTE PITSVIHPFA
EEVVYFVLLA IPILSTVATG TVSVVTANGY LVYIDFMNYL GHCNFELVPK CLFHVFPPLK
YLLYTPSFHS LHHTQFRTNY SLFMPVYDYI YGTTDKSSDE LYERTLQGRD EAAWRPDVVH
LTHLTAPESV FHNRLGFAAV ASNPLGAAAS GHLLRAASAV ASPLLSLFAS TFRSEANRLD
KLNIETWVIP RFTSHYTSKS DGYKVSRLIE KAVSDAEASG ARVLTLGLLN QGYDLNRNGE
LYVVRKPSLK TKIVDGTSLA VAAVLNMIPQ GTKDVLLLGN ANKISLVLTL SLCKREIQVR
MVNKELYECL KQQLQPEMQE HLVLSRSYSS KVWLVGDGVT DEEQMKAQKG SHFVPYSQFP
PNKARNDCVY HCTPALLVPE SFENLHVCEN WLPRRVMSAW RAAGIVHALE KWDGHECGGR
VTGVQKAWSA ALARGFRPYD DHHHPGITHD GRGGL
