HIS1B_ARATH
ID HIS1B_ARATH Reviewed; 413 AA.
AC Q8GSJ1; Q8L9K8; Q9SLW4;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=ATP phosphoribosyltransferase 2, chloroplastic;
DE Short=ATP-PRTase 2;
DE Short=AtATP-PRT2;
DE EC=2.4.2.17;
DE Flags: Precursor;
GN Name=HISN1B; OrderedLocusNames=At1g09795; ORFNames=F21M12.39;
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], CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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).
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=0.57 uM for 5-phospho-alpha-D-ribose 1-diphosphate
CC {ECO:0000269|PubMed:10712555};
CC KM=0.51 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 -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC subfamily. {ECO:0000305}.
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DR EMBL; AB025250; BAA89269.1; -; mRNA.
DR EMBL; AC000132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE28494.1; -; Genomic_DNA.
DR EMBL; AK118503; BAC43107.1; -; mRNA.
DR EMBL; BT002054; AAN72065.1; -; mRNA.
DR EMBL; BT008501; AAP37860.1; -; mRNA.
DR EMBL; AY088378; AAM65917.1; -; mRNA.
DR RefSeq; NP_563853.1; NM_100852.2.
DR AlphaFoldDB; Q8GSJ1; -.
DR SMR; Q8GSJ1; -.
DR STRING; 3702.AT1G09795.1; -.
DR iPTMnet; Q8GSJ1; -.
DR MetOSite; Q8GSJ1; -.
DR SwissPalm; Q8GSJ1; -.
DR PaxDb; Q8GSJ1; -.
DR PRIDE; Q8GSJ1; -.
DR ProteomicsDB; 230344; -.
DR EnsemblPlants; AT1G09795.1; AT1G09795.1; AT1G09795.
DR GeneID; 837509; -.
DR Gramene; AT1G09795.1; AT1G09795.1; AT1G09795.
DR KEGG; ath:AT1G09795; -.
DR Araport; AT1G09795; -.
DR TAIR; locus:505006113; AT1G09795.
DR eggNOG; KOG2831; Eukaryota.
DR HOGENOM; CLU_038115_0_0_1; -.
DR InParanoid; Q8GSJ1; -.
DR OMA; LRMVTSC; -.
DR OrthoDB; 842823at2759; -.
DR PhylomeDB; Q8GSJ1; -.
DR BioCyc; MetaCyc:AT1G09795-MON; -.
DR UniPathway; UPA00031; UER00006.
DR PRO; PR:Q8GSJ1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GSJ1; baseline and differential.
DR Genevisible; Q8GSJ1; 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 HAMAP; MF_00079; HisG_Long; 1.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR InterPro; IPR020621; ATP_PRibTrfase_HisG_long.
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 Amino-acid biosynthesis; Chloroplast; Glycosyltransferase;
KW Histidine biosynthesis; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..413
FT /note="ATP phosphoribosyltransferase 2, chloroplastic"
FT /id="PRO_0000422874"
FT CONFLICT 131
FT /note="K -> Q (in Ref. 1; BAA89269)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="P -> S (in Ref. 1; BAA89269)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="A -> P (in Ref. 1; BAA89269)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="A -> P (in Ref. 1; BAA89269)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="S -> T (in Ref. 1; BAA89269)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="H -> D (in Ref. 6; AAM65917)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 44756 MW; 155CADAE831FB1B2 CRC64;
MPISIPLNAT LQYSSPSSSS SSSSLVPSSP LFSPIPSTTV SLTGIRQRCL RMVTSCVSNA
QKSVLNGATD SVSVVGREQI RLGLPSKGRM AADSLDLLKD CQLFVKQVNP RQYVAQIPQL
PNTEVWFQRP KDIVRKLLSG DLDLGIVGLD IVGEFGQGNE DLIIVHEALN FGDCHLSLAI
PNYGIFENIK SLKELAQMPQ WTEERPLRVA TGFTYLGPKF MKDNGIKHVT FSTADGALEA
APAMGIADAI LDLVSSGTTL KENNLKEIEG GVVLESQAAL VASRRALTER KGALETVHEI
LERLEAHLKA NGQFTVVANM RGTDAEEVAE RVKTQPSLSG LQGPTISPVY CKRDGKVTIE
YYAIVICVPK KALYESVQQL RAVGGSGVLV SPVTYIFHEE TPRWSQLLSN LGL
