GLO11_ORYSI
ID GLO11_ORYSI Reviewed; 619 AA.
AC A2Z1F5;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Very-long-chain aldehyde decarbonylase GL1-1 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE AltName: Full=Protein GLOSSY 1-1 {ECO:0000305};
GN Name=GL1-1 {ECO:0000305}; ORFNames=OsI_31436 {ECO:0000312|EMBL:EAZ09166.1};
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; CM000134; EAZ09166.1; -; Genomic_DNA.
DR AlphaFoldDB; A2Z1F5; -.
DR SMR; A2Z1F5; -.
DR STRING; 39946.A2Z1F5; -.
DR EnsemblPlants; BGIOSGA030792-TA; BGIOSGA030792-PA; BGIOSGA030792.
DR Gramene; BGIOSGA030792-TA; BGIOSGA030792-PA; BGIOSGA030792.
DR HOGENOM; CLU_017842_2_0_1; -.
DR OMA; AMWAWAK; -.
DR Proteomes; UP000007015; Chromosome 9.
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; 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..619
FT /note="Very-long-chain aldehyde decarbonylase GL1-1"
FT /id="PRO_0000445869"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 129..269
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
SQ SEQUENCE 619 AA; 69657 MW; 6F79C99EF43970B4 CRC64;
MGAAFLSSWP WDNLGAYKYV LYAPLVGKAV AGRAWERASP DHWLLLLLVL FGVRALTYQL
WSSFSNMLFA TRRRRIVRDG VDFGQIDREW DWDNFLILQV HMAAAAFYAF PSLRHLPLWD
ARGLAVAALL HVAATEPLFY AAHRAFHRGH LFSCYHLQHH SAKVPQPFTA GFATPLEQLV
LGALMAVPLA AACAAGHGSV ALAFAYVLGF DNLRAMGHCN VEVFPGGLFQ SLPVLKYLIY
TPTYHTIHHT KEDANFCLFM PLFDLIGGTL DAQSWEMQKK TSAGVDEVPE FVFLAHVVDV
MQSLHVPFVL RTFASTPFSV QPFLLPMWPF AFLVMLMMWA WSKTFVISCY RLRGRLHQMW
AVPRYGFHYF LPFAKDGINN QIELAILRAD KMGAKVVSLA ALNKNEALNG GGTLFVNKHP
GLRVRVVHGN TLTAAVILNE IPQGTTEVFM TGATSKLGRA IALYLCRKKV RVMMMTLSTE
RFQKIQREAT PEHQQYLVQV TKYRSAQHCK TWIVGKWLSP REQRWAPPGT HFHQFVVPPI
IGFRRDCTYG KLAAMRLPKD VQGLGACEYS LERGVVHACH AGGVVHFLEG YTHHEVGAID
VDRIDVVWEA ALRHGLRPV
