HIS3_ARATH
ID HIS3_ARATH Reviewed; 304 AA.
AC O82782;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase, chloroplastic;
DE EC=5.3.1.16 {ECO:0000269|PubMed:9747713};
DE AltName: Full=5-proFAR isomerase;
DE AltName: Full=BBM II isomerase {ECO:0000303|PubMed:9747713};
DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase;
DE AltName: Full=Protein ALBINO AND PALE GREEN 10;
DE AltName: Full=Protein HISTIDINE BIOSYNTHESIS 3;
DE Flags: Precursor;
GN Name=HISN3; Synonyms=APG10; OrderedLocusNames=At2g36230; ORFNames=F2H17.16;
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, AND PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=9747713; DOI=10.1007/s004380050807;
RA Fujimori K., Tada S., Kanai S., Ohta D.;
RT "Molecular cloning and characterization of the gene encoding N'-[(5'-
RT phosphoribosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide
RT (BBM II) isomerase from Arabidopsis thaliana.";
RL Mol. Gen. Genet. 259:216-223(1998).
RN [2]
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 [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 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)-5-[(5-phospho-beta-D-
CC ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-
CC phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:15469,
CC ChEBI:CHEBI:58435, ChEBI:CHEBI:58525; EC=5.3.1.16;
CC Evidence={ECO:0000269|PubMed:9747713};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15470;
CC Evidence={ECO:0000269|PubMed:9747713};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
CC {ECO:0000269|PubMed:9747713}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
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DR EMBL; AB008929; BAA32457.1; -; Genomic_DNA.
DR EMBL; AB006139; BAA32456.1; -; mRNA.
DR EMBL; AC006921; AAD21442.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09219.1; -; Genomic_DNA.
DR EMBL; AK118659; BAC43255.1; -; mRNA.
DR EMBL; AY140058; AAM98199.1; -; mRNA.
DR EMBL; BT002552; AAO00912.1; -; mRNA.
DR PIR; T51822; T51822.
DR RefSeq; NP_181165.1; NM_129181.4.
DR AlphaFoldDB; O82782; -.
DR SMR; O82782; -.
DR IntAct; O82782; 1.
DR STRING; 3702.AT2G36230.1; -.
DR PaxDb; O82782; -.
DR PRIDE; O82782; -.
DR ProteomicsDB; 230336; -.
DR EnsemblPlants; AT2G36230.1; AT2G36230.1; AT2G36230.
DR GeneID; 818195; -.
DR Gramene; AT2G36230.1; AT2G36230.1; AT2G36230.
DR KEGG; ath:AT2G36230; -.
DR Araport; AT2G36230; -.
DR TAIR; locus:2049470; AT2G36230.
DR eggNOG; KOG3055; Eukaryota.
DR HOGENOM; CLU_065050_0_1_1; -.
DR InParanoid; O82782; -.
DR OMA; MTKFRPC; -.
DR OrthoDB; 1125051at2759; -.
DR PhylomeDB; O82782; -.
DR BioCyc; ARA:AT2G36230-MON; -.
DR BioCyc; MetaCyc:AT2G36230-MON; -.
DR BRENDA; 5.3.1.16; 399.
DR UniPathway; UPA00031; UER00009.
DR PRO; PR:O82782; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82782; baseline and differential.
DR Genevisible; O82782; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IDA:TAIR.
DR GO; GO:0000105; P:histidine biosynthetic process; IDA:TAIR.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011858; His6-like_euk.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR044524; Isoase_HisA-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR43090; PTHR43090; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR02129; hisA_euk; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Chloroplast; Histidine biosynthesis; Isomerase;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 62..304
FT /note="1-(5-phosphoribosyl)-5-[(5-
FT phosphoribosylamino)methylideneamino] imidazole-4-
FT carboxamide isomerase, chloroplastic"
FT /id="PRO_0000013445"
SQ SEQUENCE 304 AA; 33365 MW; AB17690E4635721B CRC64;
MRTLSSQLYS NGGLTWFQKK NQSSLFIKHL RVSKPSRVQL ISAVQFRPCI DIHKGKVKQI
VGSTLRDLKE DGSVLVTNFE SDKSAEEYAK MYKEDGLTGG HVIMLGADPL SQAAAIGALH
AYPGGLQVGG GINSENCMSY IEEGASHVIV TSYVFNNGKI DLERLKDIVS IVGKQRLILD
LSCRKKDGRY AIVTDRWQKF SDVILDEKSL EFLGGFSDEF LVHGVDVEGK KLGIDEELVA
LLGNYSPIPV TYAGGVTVMD DVERIKDAGK GRVDVTVGSA LDIFGGNLPY KDVVAWHHKQ
HSLH
