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Biotin--protein ligase 1, chloroplastic (EC 6.3.4.-) (Holocarboxylase synthetase 1) [Includes: Biotin--[methylcrotonoyl-CoA-carboxylase] ligase (EC 6.3.4.11); Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)]

 HCS1_ARATH              Reviewed;         367 AA.
Q9SL92; P92975; Q8S4V8;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 2.
25-OCT-2017, entry version 114.
RecName: Full=Biotin--protein ligase 1, chloroplastic;
EC=6.3.4.-;
AltName: Full=Holocarboxylase synthetase 1;
Includes:
RecName: Full=Biotin--[methylcrotonoyl-CoA-carboxylase] ligase;
EC=6.3.4.11;
Includes:
RecName: Full=Biotin--[acetyl-CoA-carboxylase] ligase;
EC=6.3.4.15;
Flags: Precursor;
Name=HCS1; OrderedLocusNames=At2g25710; ORFNames=F3N11.16;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=9173880; DOI=10.1042/bj3230179;
Tissot G., Douce R., Alban C.;
"Evidence for multiple forms of biotin holocarboxylase synthetase in
pea (Pisum sativum) and in Arabidopsis thaliana: subcellular
fractionation studies and isolation of a cDNA clone.";
Biochem. J. 323:179-188(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Wassilewskija;
PubMed=11784724; DOI=10.1074/jbc.M111110200;
Denis L., Grossemy M., Douce R., Alban C.;
"Molecular characterization of a second copy of holocarboxylase
synthetase gene (hcs2) in Arabidopsis thaliana.";
J. Biol. Chem. 277:10435-10444(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Shinn P., Chen H., Kim C.J., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=9874227; DOI=10.1046/j.1432-1327.1998.2580586.x;
Tissot G., Pepin R., Job D., Douce R., Alban C.;
"Purification and properties of the chloroplastic form of biotin
holocarboxylase synthetase from Arabidopsis thaliana overexpressed in
Escherichia coli.";
Eur. J. Biochem. 258:586-596(1998).
[7]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ALTERNATIVE
INITIATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=18156294; DOI=10.1104/pp.107.111534;
Puyaubert J., Denis L., Alban C.;
"Dual targeting of Arabidopsis holocarboxylase synthetase1: a small
upstream open reading frame regulates translation initiation and
protein targeting.";
Plant Physiol. 146:478-491(2008).
-!- FUNCTION: Plays a major role in biotin-dependent carboxylase
biotinylation. Catalyzes the addition of biotin to the biotin
carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase
and can also biotinylate methylcrotonyl-CoA carboxylase. Is
responsible for most, if not all, biotin--protein ligase activity
in Arabidopsis. Is essential for plant viability and required for
ovule development. {ECO:0000269|PubMed:18156294,
ECO:0000269|PubMed:9173880, ECO:0000269|PubMed:9874227}.
-!- CATALYTIC ACTIVITY: ATP + biotin + apo-[3-methylcrotonoyl-
CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [3-
methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)].
-!- CATALYTIC ACTIVITY: ATP + biotin + apo-[acetyl-CoA:carbon-dioxide
ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-
dioxide ligase (ADP-forming)].
-!- SUBCELLULAR LOCATION: Isoform HCS-ATG1: Plastid, chloroplast
{ECO:0000269|PubMed:18156294}.
-!- SUBCELLULAR LOCATION: Isoform HCS-ATG2: Cytoplasm, cytosol
{ECO:0000269|PubMed:18156294}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=HCS-ATG1;
IsoId=Q9SL92-1; Sequence=Displayed;
Name=HCS-ATG2;
IsoId=Q9SL92-2; Sequence=VSP_053916;
-!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers,
siliques and seeds. {ECO:0000269|PubMed:11784724,
ECO:0000269|PubMed:18156294}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous due to
aborted ovules that had not been fertilized.
{ECO:0000269|PubMed:18156294}.
-!- MISCELLANEOUS: The alternative splicing of the 5'UTR of HCS1 mRNA
controls the dual targeting of HCS1 protein through alternative
use of distinct initiation codons. A small ORF (uORF24) located in
the HCS1 mRNA 5'UTR is essential for the AUG choice. The presence
of uORF24 favors the synthesis of a short protein form initiated
at the second AUG, which consequently localizes in the cytosol. In
the absence of uORF24, the translation initiation begins at the
first AUG, allowing the production of a HCS1 protein headed by a
transit peptide (PubMed:18156294). {ECO:0000305|PubMed:18156294}.
-!- SIMILARITY: Belongs to the biotin--protein ligase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U41369; AAC49706.1; -; mRNA.
EMBL; AF414937; AAL93108.1; -; Genomic_DNA.
EMBL; AC006053; AAD31371.2; -; Genomic_DNA.
EMBL; CP002685; AEC07740.1; -; Genomic_DNA.
EMBL; CP002685; AEC07741.1; -; Genomic_DNA.
EMBL; CP002685; ANM62688.1; -; Genomic_DNA.
EMBL; CP002685; ANM62689.1; -; Genomic_DNA.
EMBL; BT024748; ABD59086.1; -; mRNA.
PIR; G84651; G84651.
RefSeq; NP_001324829.1; NM_001336012.1. [Q9SL92-2]
RefSeq; NP_001324830.1; NM_001336013.1. [Q9SL92-2]
RefSeq; NP_565605.1; NM_128130.3. [Q9SL92-1]
RefSeq; NP_850067.1; NM_179736.1. [Q9SL92-1]
UniGene; At.19972; -.
ProteinModelPortal; Q9SL92; -.
STRING; 3702.AT2G25710.1; -.
iPTMnet; Q9SL92; -.
PaxDb; Q9SL92; -.
EnsemblPlants; AT2G25710.1; AT2G25710.1; AT2G25710. [Q9SL92-1]
EnsemblPlants; AT2G25710.2; AT2G25710.2; AT2G25710. [Q9SL92-1]
EnsemblPlants; AT2G25710.4; AT2G25710.4; AT2G25710. [Q9SL92-2]
EnsemblPlants; AT2G25710.5; AT2G25710.5; AT2G25710. [Q9SL92-2]
GeneID; 817112; -.
Gramene; AT2G25710.1; AT2G25710.1; AT2G25710.
Gramene; AT2G25710.2; AT2G25710.2; AT2G25710.
Gramene; AT2G25710.4; AT2G25710.4; AT2G25710.
Gramene; AT2G25710.5; AT2G25710.5; AT2G25710.
KEGG; ath:AT2G25710; -.
Araport; AT2G25710; -.
TAIR; locus:2050291; AT2G25710.
eggNOG; KOG1536; Eukaryota.
eggNOG; COG0340; LUCA.
HOGENOM; HOG000264536; -.
InParanoid; Q9SL92; -.
KO; K01942; -.
OMA; CAKGLSE; -.
OrthoDB; EOG09360GI8; -.
PhylomeDB; Q9SL92; -.
BioCyc; ARA:AT2G25710-MONOMER; -.
BioCyc; MetaCyc:AT2G25710-MONOMER; -.
Reactome; R-ATH-196780; Biotin transport and metabolism.
PRO; PR:Q9SL92; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q9SL92; baseline and differential.
Genevisible; Q9SL92; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0009536; C:plastid; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IDA:TAIR.
GO; GO:0004078; F:biotin-[methylcrotonoyl-CoA-carboxylase] ligase activity; IDA:TAIR.
GO; GO:0042966; P:biotin carboxyl carrier protein biosynthetic process; IDA:TAIR.
GO; GO:0006464; P:cellular protein modification process; IEA:InterPro.
CDD; cd16442; BPL; 1.
InterPro; IPR004408; Biotin_CoA_COase_ligase.
InterPro; IPR003142; BPL_C.
InterPro; IPR004143; BPL_LPL_catalytic.
PANTHER; PTHR12835:SF5; PTHR12835:SF5; 1.
Pfam; PF02237; BPL_C; 1.
Pfam; PF03099; BPL_LplA_LipB; 1.
TIGRFAMs; TIGR00121; birA_ligase; 1.
PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
1: Evidence at protein level;
Alternative initiation; ATP-binding; Chloroplast; Complete proteome;
Cytoplasm; Ligase; Multifunctional enzyme; Nucleotide-binding;
Plastid; Reference proteome; Transit peptide.
TRANSIT 1 37 Chloroplast. {ECO:0000255}.
CHAIN 38 367 Biotin--protein ligase 1, chloroplastic.
/FTId=PRO_0000425972.
DOMAIN 105 289 BPL/LPL catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01067}.
REGION 122 123 Biotin binding. {ECO:0000250}.
REGION 149 151 Biotin binding. {ECO:0000250}.
BINDING 145 145 Biotin. {ECO:0000250}.
BINDING 220 220 Biotin. {ECO:0000250}.
VAR_SEQ 1 38 Missing (in isoform HCS-ATG2).
{ECO:0000305}.
/FTId=VSP_053916.
CONFLICT 28 28 H -> R (in Ref. 2; AAL93108).
{ECO:0000305}.
SEQUENCE 367 AA; 41219 MW; BB0192B4CD2EB5CF CRC64;
MEAVRSTTTL SNFHLLNILV LRSLKPLHRL SFSFSASAME SDASCSLVLC GKSSVETEVA
KGLKNKNSLK LPDNTKVSLI LESEAKNLVK DDDNSFNLSL FMNSIITHRF GRFLIWSPRL
SSTHDVVSHN FSELPVGSVC VTDIQFKGRG RTKNVWESPK GCLMYSFTLE MEDGRVVPLI
QYVVSLAVTE AVKDVCDKKG LPYIDVKIKW PNDLYVNGLK VGGILCTSTY RSKKFNVSVG
VGLNVDNGQP TTCLNAVLKG MAPESNLLKR EEILGAFFHK FEKFFDLFMD QGFKSLEELY
YRTWLHSEQR VIVEDKVEDQ VVQNVVTIQG LTSSGYLLAV GDDNQMYELH PDGNSFDFFK
GLVRRKI


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