LCB1B_ORYSJ
ID LCB1B_ORYSJ Reviewed; 481 AA.
AC Q6K8E7; A0A0P0VQY7; Q0DWM3;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Long chain base biosynthesis protein 1b;
DE EC=2.3.1.50;
GN OrderedLocusNames=Os02g0806900, LOC_Os02g56300;
GN ORFNames=OJ1111_C07.25, OsJ_08792;
OS Oryza sativa subsp. japonica (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=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer formed
CC with LCB2 constitutes the catalytic core (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexadecanoyl-CoA + L-serine = 3-oxosphinganine + CO2 +
CC CoA; Xref=Rhea:RHEA:14761, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58299; EC=2.3.1.50;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC -!- SUBUNIT: Heterodimer with LCB2. Component of the serine
CC palmitoyltransferase (SPT) complex, composed of LCB1 and LCB2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AP004153; BAD19391.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF10365.2; -; Genomic_DNA.
DR EMBL; AP014958; BAS81479.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE58013.1; -; Genomic_DNA.
DR EMBL; AK073935; BAG93720.1; -; mRNA.
DR EMBL; AK105851; BAG97394.1; -; mRNA.
DR RefSeq; XP_015622652.1; XM_015767166.1.
DR AlphaFoldDB; Q6K8E7; -.
DR SMR; Q6K8E7; -.
DR STRING; 4530.OS02T0806900-01; -.
DR PaxDb; Q6K8E7; -.
DR PRIDE; Q6K8E7; -.
DR EnsemblPlants; Os02t0806900-01; Os02t0806900-01; Os02g0806900.
DR GeneID; 4331075; -.
DR Gramene; Os02t0806900-01; Os02t0806900-01; Os02g0806900.
DR KEGG; osa:4331075; -.
DR eggNOG; KOG1358; Eukaryota.
DR HOGENOM; CLU_015846_0_1_1; -.
DR InParanoid; Q6K8E7; -.
DR OMA; IVIRHAI; -.
DR OrthoDB; 438936at2759; -.
DR PlantReactome; R-OSA-1119325; Sphingolipid metabolism.
DR PlantReactome; R-OSA-1119610; Biotin biosynthesis II.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6K8E7; OS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Lipid metabolism; Membrane;
KW Pyridoxal phosphate; Reference proteome; Sphingolipid metabolism;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..481
FT /note="Long chain base biosynthesis protein 1b"
FT /id="PRO_0000419148"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 481 AA; 52010 MW; 42942D30AAF65F18 CRC64;
MEMVLPVANA TAAALARVSA MFNAPLARAV VFGIHIDGHL VVEGLLIAAI LFQLSRKSYK
PPKKPLTERE VDELCDEWQP EPLCPPIKEG ARIEAPTLES AAGPHTIVDG KEVVNFASAN
YLGLIGNEKI LDSCIGSVEK YGVGSCGPRG FYGTIDVHLD CETKIAKFLG TQDSILYSYG
ISTIFSVIPA FCKKGDIIVA DEGVHWAVQN GLQLSRSTVV YFKHNDMASL ASTLEKLTHG
NKRTEKIRRY IVVEAIYQNS GQIAPLDEIV RLKEKYRFRV ILEESHSFGV LGKSGRGLAE
HYGVPIEKID IITAGMGNAL ATDGGFCTGS IRVVDHQRLS SSGYVFSASL PPYLASAAIS
AVDHLEENPS VLANLRSNIT LLHKELSDVQ GLEIASNILS PIVFLKLKTS TGSAVADLEL
LEVISEKVLK EDSVFIAATK RSSLDKCRLP VGIRLFVSAG HTESDILKVS ESLKRVAASV
L
