HCS1_ARATH
ID HCS1_ARATH Reviewed; 367 AA.
AC Q9SL92; P92975; Q8S4V8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Biotin--protein ligase 1, chloroplastic {ECO:0000305};
DE EC=6.3.4.- {ECO:0000269|PubMed:9874227};
DE AltName: Full=Holocarboxylase synthetase 1 {ECO:0000303|PubMed:18156294};
DE Includes:
DE RecName: Full=Biotin--[methylcrotonoyl-CoA-carboxylase] ligase {ECO:0000303|PubMed:9874227};
DE EC=6.3.4.11 {ECO:0000269|PubMed:18156294, ECO:0000269|PubMed:9874227};
DE Includes:
DE RecName: Full=Biotin--[acetyl-CoA-carboxylase] ligase {ECO:0000303|PubMed:9874227};
DE EC=6.3.4.15 {ECO:0000269|PubMed:18156294, ECO:0000269|PubMed:9874227};
DE Flags: Precursor;
GN Name=HCS1 {ECO:0000303|PubMed:18156294};
GN OrderedLocusNames=At2g25710 {ECO:0000312|Araport:AT2G25710};
GN ORFNames=F3N11.16 {ECO:0000312|EMBL:AAD31371.2};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=9173880; DOI=10.1042/bj3230179;
RA Tissot G., Douce R., Alban C.;
RT "Evidence for multiple forms of biotin holocarboxylase synthetase in pea
RT (Pisum sativum) and in Arabidopsis thaliana: subcellular fractionation
RT studies and isolation of a cDNA clone.";
RL Biochem. J. 323:179-188(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11784724; DOI=10.1074/jbc.m111110200;
RA Denis L., Grossemy M., Douce R., Alban C.;
RT "Molecular characterization of a second copy of holocarboxylase synthetase
RT gene (hcs2) in Arabidopsis thaliana.";
RL J. Biol. Chem. 277:10435-10444(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9874227; DOI=10.1046/j.1432-1327.1998.2580586.x;
RA Tissot G., Pepin R., Job D., Douce R., Alban C.;
RT "Purification and properties of the chloroplastic form of biotin
RT holocarboxylase synthetase from Arabidopsis thaliana overexpressed in
RT Escherichia coli.";
RL Eur. J. Biochem. 258:586-596(1998).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ALTERNATIVE INITIATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18156294; DOI=10.1104/pp.107.111534;
RA Puyaubert J., Denis L., Alban C.;
RT "Dual targeting of Arabidopsis holocarboxylase synthetase1: a small
RT upstream open reading frame regulates translation initiation and protein
RT targeting.";
RL Plant Physiol. 146:478-491(2008).
CC -!- FUNCTION: Plays a major role in biotin-dependent carboxylase
CC biotinylation (PubMed:18156294). Catalyzes the addition of biotin to
CC the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA
CC carboxylase (PubMed:9173880, PubMed:9874227, PubMed:18156294). Can also
CC biotinylate methylcrotonyl-CoA carboxylase (PubMed:9874227,
CC PubMed:18156294). Is responsible for most, if not all, biotin--protein
CC ligase activity in Arabidopsis (PubMed:18156294). Is essential for
CC plant viability and required for ovule development (PubMed:18156294).
CC {ECO:0000269|PubMed:18156294, ECO:0000269|PubMed:9173880,
CC ECO:0000269|PubMed:9874227}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-
CC forming)] + ATP + biotin = AMP + diphosphate + H(+) + holo-[3-
CC methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)];
CC Xref=Rhea:RHEA:24376, Rhea:RHEA-COMP:10514, Rhea:RHEA-COMP:10515,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57586, ChEBI:CHEBI:83144,
CC ChEBI:CHEBI:456215; EC=6.3.4.11;
CC Evidence={ECO:0000269|PubMed:18156294, ECO:0000269|PubMed:9874227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24377;
CC Evidence={ECO:0000269|PubMed:18156294, ECO:0000269|PubMed:9874227};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) +
CC N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215;
CC EC=6.3.4.15; Evidence={ECO:0000269|PubMed:18156294,
CC ECO:0000269|PubMed:9874227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11757;
CC Evidence={ECO:0000269|PubMed:18156294, ECO:0000269|PubMed:9874227};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 uM for biotin {ECO:0000269|PubMed:9874227};
CC KM=4.4 uM for ATP {ECO:0000269|PubMed:9874227};
CC KM=32 uM for methylcrotonoyl-CoA carboxylase
CC {ECO:0000269|PubMed:9874227};
CC Vmax=115 nmol/min/mg enzyme with biotin as substrate
CC {ECO:0000269|PubMed:9874227};
CC Vmax=127 nmol/min/mg enzyme with ATP as substrate
CC {ECO:0000269|PubMed:9874227};
CC Vmax=130 nmol/min/mg enzyme with methylcrotonoyl-CoA carboxylase as
CC substrate {ECO:0000269|PubMed:9874227};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Plastid, chloroplast
CC {ECO:0000269|PubMed:18156294}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:18156294}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=HCS-ATG1 {ECO:0000303|PubMed:18156294};
CC IsoId=Q9SL92-1; Sequence=Displayed;
CC Name=2; Synonyms=HCS-ATG2 {ECO:0000303|PubMed:18156294};
CC IsoId=Q9SL92-2; Sequence=VSP_053916;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers,
CC siliques and seeds. {ECO:0000269|PubMed:11784724,
CC ECO:0000269|PubMed:18156294}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous due to
CC aborted ovules that had not been fertilized.
CC {ECO:0000269|PubMed:18156294}.
CC -!- MISCELLANEOUS: The alternative splicing of the 5'UTR of HCS1 mRNA
CC controls the dual targeting of HCS1 protein through alternative use of
CC distinct initiation codons. A small ORF (uORF24) located in the HCS1
CC mRNA 5'UTR is essential for the AUG choice. The presence of uORF24
CC favors the synthesis of a short protein form initiated at the second
CC AUG, which consequently localizes in the cytosol. In the absence of
CC uORF24, the translation initiation begins at the first AUG, allowing
CC the production of a HCS1 protein headed by a transit peptide.
CC {ECO:0000269|PubMed:18156294}.
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000305}.
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DR EMBL; U41369; AAC49706.1; -; mRNA.
DR EMBL; AF414937; AAL93108.1; -; Genomic_DNA.
DR EMBL; AC006053; AAD31371.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07740.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07741.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62688.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62689.1; -; Genomic_DNA.
DR EMBL; BT024748; ABD59086.1; -; mRNA.
DR PIR; G84651; G84651.
DR RefSeq; NP_001324829.1; NM_001336012.1. [Q9SL92-2]
DR RefSeq; NP_001324830.1; NM_001336013.1. [Q9SL92-2]
DR RefSeq; NP_565605.1; NM_128130.3. [Q9SL92-1]
DR RefSeq; NP_850067.1; NM_179736.1. [Q9SL92-1]
DR AlphaFoldDB; Q9SL92; -.
DR SMR; Q9SL92; -.
DR STRING; 3702.AT2G25710.1; -.
DR iPTMnet; Q9SL92; -.
DR PaxDb; Q9SL92; -.
DR PRIDE; Q9SL92; -.
DR ProteomicsDB; 247167; -. [Q9SL92-1]
DR EnsemblPlants; AT2G25710.1; AT2G25710.1; AT2G25710. [Q9SL92-1]
DR EnsemblPlants; AT2G25710.2; AT2G25710.2; AT2G25710. [Q9SL92-1]
DR EnsemblPlants; AT2G25710.4; AT2G25710.4; AT2G25710. [Q9SL92-2]
DR EnsemblPlants; AT2G25710.5; AT2G25710.5; AT2G25710. [Q9SL92-2]
DR GeneID; 817112; -.
DR Gramene; AT2G25710.1; AT2G25710.1; AT2G25710. [Q9SL92-1]
DR Gramene; AT2G25710.2; AT2G25710.2; AT2G25710. [Q9SL92-1]
DR Gramene; AT2G25710.4; AT2G25710.4; AT2G25710. [Q9SL92-2]
DR Gramene; AT2G25710.5; AT2G25710.5; AT2G25710. [Q9SL92-2]
DR KEGG; ath:AT2G25710; -.
DR Araport; AT2G25710; -.
DR TAIR; locus:2050291; AT2G25710.
DR eggNOG; KOG1536; Eukaryota.
DR HOGENOM; CLU_051096_2_0_1; -.
DR InParanoid; Q9SL92; -.
DR OMA; CCAKGLS; -.
DR OrthoDB; 1392751at2759; -.
DR PhylomeDB; Q9SL92; -.
DR BioCyc; ARA:AT2G25710-MON; -.
DR BioCyc; MetaCyc:AT2G25710-MON; -.
DR PRO; PR:Q9SL92; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SL92; baseline and differential.
DR Genevisible; Q9SL92; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IDA:TAIR.
DR GO; GO:0004078; F:biotin-[methylcrotonoyl-CoA-carboxylase] ligase activity; IDA:TAIR.
DR GO; GO:0042966; P:biotin carboxyl carrier protein biosynthetic process; IDA:TAIR.
DR CDD; cd16442; BPL; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR InterPro; IPR003142; BPL_C.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR Pfam; PF02237; BPL_C; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00121; birA_ligase; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; ATP-binding; Chloroplast; Cytoplasm; Ligase;
KW Multifunctional enzyme; Nucleotide-binding; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..37
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 38..367
FT /note="Biotin--protein ligase 1, chloroplastic"
FT /id="PRO_0000425972"
FT DOMAIN 105..289
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT BINDING 122..124
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000250|UniProtKB:P06709"
FT BINDING 145
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000250|UniProtKB:P06709"
FT BINDING 149..151
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000250|UniProtKB:P06709"
FT BINDING 220
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000250|UniProtKB:P06709"
FT VAR_SEQ 1..38
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053916"
FT CONFLICT 28
FT /note="H -> R (in Ref. 2; AAL93108)"
FT /evidence="ECO:0000305"
SQ 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
