HIS1A_ARATH
ID HIS1A_ARATH Reviewed; 411 AA.
AC Q9S762;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=ATP phosphoribosyltransferase 1, chloroplastic;
DE Short=ATP-PRTase 1;
DE Short=AtATP-PRT1;
DE EC=2.4.2.17;
DE Flags: Precursor;
GN Name=HISN1A; OrderedLocusNames=At1g58080; ORFNames=T15M6.9;
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 [GENOMIC DNA / MRNA], CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=10712555; DOI=10.1104/pp.122.3.907;
RA Ohta D., Fujimori K., Mizutani M., Nakayama Y., Kunpaisal-Hashimoto R.,
RA Munzer S., Kozaki A.;
RT "Molecular cloning and characterization of ATP-phosphoribosyl transferase
RT from Arabidopsis, a key enzyme in the histidine biosynthetic pathway.";
RL Plant Physiol. 122:907-914(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16547652; DOI=10.1007/s00726-005-0247-0;
RA Stepansky A., Leustek T.;
RT "Histidine biosynthesis in plants.";
RL Amino Acids 30:127-142(2006).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17434988; DOI=10.1104/pp.107.096511;
RA Muralla R., Sweeney C., Stepansky A., Leustek T., Meinke D.;
RT "Genetic dissection of histidine biosynthesis in Arabidopsis.";
RL Plant Physiol. 144:890-903(2007).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-50, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER CYS-49, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-
CC diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-
CC alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017,
CC ChEBI:CHEBI:73183; EC=2.4.2.17;
CC Evidence={ECO:0000269|PubMed:10712555};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Feedback inhibited by L-histidine. {ECO:0000305}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.19 uM for 5-phospho-alpha-D-ribose 1-diphosphate
CC {ECO:0000269|PubMed:10712555};
CC KM=0.6 uM for ATP {ECO:0000269|PubMed:10712555};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and at lower levels in roots
CC (at protein level). {ECO:0000269|PubMed:10712555}.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC subfamily. {ECO:0000305}.
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DR EMBL; AB025249; BAA89268.1; -; mRNA.
DR EMBL; AB025251; BAA89270.1; -; Genomic_DNA.
DR EMBL; AC079604; AAG50704.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33495.1; -; Genomic_DNA.
DR EMBL; AY093018; AAM13017.1; -; mRNA.
DR EMBL; AY128941; AAM91341.1; -; mRNA.
DR PIR; T51818; T51818.
DR RefSeq; NP_176105.1; NM_104590.4.
DR AlphaFoldDB; Q9S762; -.
DR SMR; Q9S762; -.
DR STRING; 3702.AT1G58080.1; -.
DR iPTMnet; Q9S762; -.
DR MetOSite; Q9S762; -.
DR PaxDb; Q9S762; -.
DR PRIDE; Q9S762; -.
DR ProteomicsDB; 230132; -.
DR EnsemblPlants; AT1G58080.1; AT1G58080.1; AT1G58080.
DR GeneID; 842175; -.
DR Gramene; AT1G58080.1; AT1G58080.1; AT1G58080.
DR KEGG; ath:AT1G58080; -.
DR Araport; AT1G58080; -.
DR TAIR; locus:2196287; AT1G58080.
DR eggNOG; KOG2831; Eukaryota.
DR HOGENOM; CLU_038115_0_0_1; -.
DR InParanoid; Q9S762; -.
DR OMA; VDYYAIV; -.
DR OrthoDB; 842823at2759; -.
DR PhylomeDB; Q9S762; -.
DR BioCyc; MetaCyc:AT1G58080-MON; -.
DR BRENDA; 2.4.2.17; 399.
DR UniPathway; UPA00031; UER00006.
DR PRO; PR:Q9S762; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S762; baseline and differential.
DR Genevisible; Q9S762; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IDA:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IDA:TAIR.
DR Gene3D; 3.30.70.120; -; 1.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR InterPro; IPR013115; HisG_C.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR PANTHER; PTHR21403; PTHR21403; 1.
DR Pfam; PF01634; HisG; 1.
DR Pfam; PF08029; HisG_C; 1.
DR SUPFAM; SSF54913; SSF54913; 1.
DR TIGRFAMs; TIGR00070; hisG; 1.
DR TIGRFAMs; TIGR03455; HisG_C-term; 1.
DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis; Chloroplast; Histidine biosynthesis;
KW Plastid; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 50..411
FT /note="ATP phosphoribosyltransferase 1, chloroplastic"
FT /id="PRO_0000422873"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 411 AA; 44556 MW; CDECF379CFC1A5C4 CRC64;
MSLLLPTNLQ QYPSSSSFPS STPILSPPPS TAFSVIVPRR RCLRLVTSCV STVQSSVATN
GSSPAPAPAA VVVERDQIRL GLPSKGRMAA DAIDLLKDCQ LFVKQVNPRQ YVAQIPQLPN
TEVWFQRPKD IVRKLLSGDL DLGIVGLDTL SEYGQENEDL IIVHEALNFG DCHLSIAIPN
YGIFENINSL KELAQMPQWS EERPLRLATG FTYLGPKFMK ENGIKHVVFS TADGALEAAP
AMGIADAILD LVSSGITLKE NNLKEIEGGV VLESQAALVA SRRALNERKG ALNTVHEILE
RLEAHLKADG QFTVVANMRG NSAQEVAERV LSQPSLSGLQ GPTISPVYCT QNGKVSVDYY
AIVICVPKKA LYDSVKQLRA AGGSGVLVSP LTYIFDEDTP RWGQLLRNLG I
