GLO14_ORYSI
ID GLO14_ORYSI Reviewed; 619 AA.
AC B8AFI3;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Very-long-chain aldehyde decarbonylase GL1-4 {ECO:0000305};
DE EC=4.1.99.5 {ECO:0000250|UniProtKB:F4HVY0};
DE AltName: Full=Protein GLOSSY 1-4 {ECO:0000305};
GN Name=GL1-4 {ECO:0000305}; ORFNames=OsI_08114 {ECO:0000312|EMBL:EEC73617.1};
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; EEC73617.1; -; Genomic_DNA.
DR AlphaFoldDB; B8AFI3; -.
DR STRING; 39946.B8AFI3; -.
DR EnsemblPlants; BGIOSGA006020-TA; BGIOSGA006020-PA; BGIOSGA006020.
DR Gramene; BGIOSGA006020-TA; BGIOSGA006020-PA; BGIOSGA006020.
DR HOGENOM; CLU_017842_1_0_1; -.
DR OMA; SIYSFFM; -.
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:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0009409; P:response to cold; 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..619
FT /note="Very-long-chain aldehyde decarbonylase GL1-4"
FT /id="PRO_0000445874"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 138..272
FT /note="Fatty acid hydroxylase"
FT /evidence="ECO:0000255"
SQ SEQUENCE 619 AA; 71509 MW; B3EFB9FE5A0C87AA CRC64;
MATRPGPLTE WPWHRLGNFK YVVMAPVVAH GARRVMRNGW GDLDIAFSLI LPSLLLRMIH
NQIWISLSRY QTARSKHRIV DRGIEFDQVD RERGWDDQIL FNGLVFYAGY LAMPSVRRMP
VWRTDGAVVT ALVHTGPVEF LYYWFHRALH HHFLYSRYHS HHHASIVTEP ITSVIHPFAE
HVVYFILFAI PILSTIYLGN VSAMGIVGYI AYIDFMNNMG HCNFELVPEW IFQIFPPLKY
LIYTPSFHSL HHTQFRTNYS LFMPFYDYIY NTMDKSSDEL YESSLKGTEE TPDLVHLTHM
TNLQSAYHLR IGIASIASKP YSDSAWYMWT LWPLAWLSMV LAWIYGSSAF VVERIKLNKM
KMQTWAIPRY NFQYGLTWER EPINDLIEKA ILDADMKGVK VISLGLLNQA KQLNGNGELF
RQKYPKLGVR IVDGSGLATA VVLKSIPSDA KKVFLRTGTS KIARAIAIAL CDRGVQVIMN
EKEVYHMLKS QIPENRASYL KLSSDNVPQL WIVHNIDDNE QKMAPKGTIF IPISQFPLKK
LRKDCTYMST PAMRIPEEMK NIHSCENWLP RRVMSAWHIA GILHALEGWN MHECGDEMMD
IEKSWSAAIR HGFLPLTKA
