HIS2_ARATH
ID HIS2_ARATH Reviewed; 281 AA.
AC O82768;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Histidine biosynthesis bifunctional protein hisIE, chloroplastic;
DE AltName: Full=Protein HISTIDINE BIOSYNTHESIS 2;
DE Includes:
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE Short=PRA-CH;
DE EC=3.5.4.19 {ECO:0000269|PubMed:9733547};
DE Includes:
DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE Short=PRA-PH;
DE EC=3.6.1.31 {ECO:0000269|PubMed:9733547};
DE Flags: Precursor;
GN Name=HISN2; OrderedLocusNames=At1g31860; ORFNames=F5M6.13;
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], FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9733547; DOI=10.1104/pp.118.1.275;
RA Fujimori K., Ohta D.;
RT "Isolation and characterization of a histidine biosynthetic gene in
RT Arabidopsis encoding a polypeptide with two separate domains for
RT phosphoribosyl-ATP pyrophosphohydrolase and phosphoribosyl-AMP
RT cyclohydrolase.";
RL Plant Physiol. 118:275-283(1998).
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 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 [6]
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 [7]
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 -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-
CC ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31;
CC Evidence={ECO:0000269|PubMed:9733547};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-
CC D-ribosyl)-5-[(5-phospho-beta-D-
CC ribosylamino)methylideneamino]imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435,
CC ChEBI:CHEBI:59457; EC=3.5.4.19;
CC Evidence={ECO:0000269|PubMed:9733547};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC {ECO:0000269|PubMed:9733547}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC {ECO:0000269|PubMed:9733547}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed throughout development.
CC {ECO:0000269|PubMed:9733547}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB006083; BAA32529.1; -; Genomic_DNA.
DR EMBL; AB006082; BAA32528.1; -; mRNA.
DR EMBL; AC079041; AAG50725.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31408.1; -; Genomic_DNA.
DR EMBL; AY046000; AAK76674.1; -; mRNA.
DR EMBL; AY079376; AAL85107.1; -; mRNA.
DR EMBL; AY086514; AAM63514.1; -; mRNA.
DR PIR; T51812; T51812.
DR RefSeq; NP_174469.1; NM_102923.4.
DR AlphaFoldDB; O82768; -.
DR SMR; O82768; -.
DR STRING; 3702.AT1G31860.1; -.
DR SwissPalm; O82768; -.
DR PaxDb; O82768; -.
DR PRIDE; O82768; -.
DR EnsemblPlants; AT1G31860.1; AT1G31860.1; AT1G31860.
DR GeneID; 840076; -.
DR Gramene; AT1G31860.1; AT1G31860.1; AT1G31860.
DR KEGG; ath:AT1G31860; -.
DR Araport; AT1G31860; -.
DR TAIR; locus:2034516; AT1G31860.
DR eggNOG; KOG4311; Eukaryota.
DR HOGENOM; CLU_048577_3_2_1; -.
DR InParanoid; O82768; -.
DR OrthoDB; 1578476at2759; -.
DR PhylomeDB; O82768; -.
DR BioCyc; ARA:AT1G31860-MON; -.
DR BioCyc; MetaCyc:AT1G31860-MON; -.
DR BRENDA; 3.5.4.19; 399.
DR UniPathway; UPA00031; UER00007.
DR UniPathway; UPA00031; UER00008.
DR PRO; PR:O82768; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O82768; baseline and differential.
DR Genevisible; O82768; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IDA:TAIR.
DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IDA:TAIR.
DR GO; GO:0000105; P:histidine biosynthetic process; TAS:TAIR.
DR CDD; cd11534; NTP-PPase_HisIE_like; 1.
DR Gene3D; 3.10.20.810; -; 1.
DR HAMAP; MF_01019; HisIE; 1.
DR InterPro; IPR023019; His_synth_HisIE.
DR InterPro; IPR008179; HisE.
DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR Pfam; PF01502; PRA-CH; 1.
DR Pfam; PF01503; PRA-PH; 1.
DR SUPFAM; SSF141734; SSF141734; 1.
DR TIGRFAMs; TIGR03188; histidine_hisI; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Chloroplast; Histidine biosynthesis;
KW Hydrolase; Multifunctional enzyme; Nucleotide-binding; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..281
FT /note="Histidine biosynthesis bifunctional protein hisIE,
FT chloroplastic"
FT /id="PRO_0000013444"
FT REGION 51..178
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT REGION 179..281
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
SQ SEQUENCE 281 AA; 31668 MW; BCD3754832959E46 CRC64;
MAVSYNALAQ SLARSSCFIP KPYSFRDTKL RSRSNVVFAC NDNKNIALQA KVDNLLDRIK
WDDKGLAVAI AQNVDTGAVL MQGFVNREAL STTISSRKAT FFSRSRSTLW TKGETSNNFI
NILDVYVDCD RDSIIYLGTP DGPTCHTGEE TCYYTSVFDQ LNNDEASGNK LALTTLYSLE
SIISKRKEES TVPQEGKPSW TRRLLTDDAL LCSKIREEAD ELCRTLEDNE EVSRTPSEMA
DVLYHAMVLL SKRGVKMEDV LEVLRKRFSQ SGIEEKQNRT K
