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Protein

Imidazoleglycerol-phosphate dehydratase 2, chloroplastic

Gene

HISN5B

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Pathwayi: L-histidine biosynthesis

This protein is involved in step 6 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase 1, chloroplastic (HISN1A), ATP phosphoribosyltransferase 2, chloroplastic (HISN1B)
  2. Histidine biosynthesis bifunctional protein hisIE, chloroplastic (HISN2)
  3. Histidine biosynthesis bifunctional protein hisIE, chloroplastic (HISN2)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase, chloroplastic (HISN3)
  5. Imidazole glycerol phosphate synthase hisHF, chloroplastic (HISN4)
  6. Imidazoleglycerol-phosphate dehydratase 2, chloroplastic (HISN5B), Imidazoleglycerol-phosphate dehydratase (HISN5B), Imidazoleglycerol-phosphate dehydratase (At3g22425), Imidazoleglycerol-phosphate dehydratase 1, chloroplastic (HISN5A), Imidazoleglycerol-phosphate dehydratase (HISN5B)
  7. Histidinol-phosphate aminotransferase 2, chloroplastic (HISN6B), Histidinol-phosphate aminotransferase 1, chloroplastic (HISN6A)
  8. Bifunctional phosphatase IMPL2, chloroplastic (HISN7)
  9. Histidinol dehydrogenase, chloroplastic (HISN8)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi112 – 1121Manganese 1By similarity
Metal bindingi138 – 1381Manganese 2By similarity
Metal bindingi139 – 1391Manganese 1By similarity
Metal bindingi142 – 1421Manganese 2By similarity
Metal bindingi210 – 2101Manganese 2By similarity
Metal bindingi234 – 2341Manganese 1By similarity
Metal bindingi235 – 2351Manganese 2By similarity
Metal bindingi238 – 2381Manganese 1By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciARA:GQT-1999-MONOMER.
ARA:GQT-2000-MONOMER.
UniPathwayiUPA00031; UER00011.

Names & Taxonomyi

Protein namesi
Recommended name:
Imidazoleglycerol-phosphate dehydratase 2, chloroplastic (EC:4.2.1.19)
Short name:
IGPD 2
Alternative name(s):
Protein HISTIDINE BIOSYNTHESIS 5B
Gene namesi
Name:HISN5B
Ordered Locus Names:At4g14910
ORF Names:dl3495c
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G14910.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5252ChloroplastSequence analysisAdd
BLAST
Chaini53 – 272220Imidazoleglycerol-phosphate dehydratase 2, chloroplasticPRO_0000158254Add
BLAST

Proteomic databases

PaxDbiO23346.
PRIDEiO23346.

Expressioni

Gene expression databases

ExpressionAtlasiO23346. baseline and differential.
GenevisibleiO23346. AT.

Interactioni

Protein-protein interaction databases

BioGridi12446. 1 interaction.
DIPiDIP-61567N.
STRINGi3702.AT4G14910.2.

Structurei

Secondary structure

1
272
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi77 – 837Combined sources
Beta strandi85 – 9410Combined sources
Beta strandi101 – 1044Combined sources
Helixi108 – 12114Combined sources
Beta strandi124 – 1318Combined sources
Turni133 – 1353Combined sources
Helixi138 – 15619Combined sources
Beta strandi165 – 1728Combined sources
Beta strandi175 – 1828Combined sources
Beta strandi188 – 1914Combined sources
Beta strandi197 – 2004Combined sources
Helixi207 – 21913Combined sources
Beta strandi222 – 2298Combined sources
Helixi233 – 25220Combined sources
Turni256 – 2605Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MU0X-ray1.30A69-272[»]
4MU1X-ray1.50A54-272[»]
4MU3X-ray1.12A69-272[»]
4MU4X-ray1.41A69-272[»]
4QNJX-ray1.30A69-272[»]
4QNKX-ray1.75A/B/C/D/E/F/G/H70-272[»]
ProteinModelPortaliO23346.
SMRiO23346. Positions 74-258.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3143. Eukaryota.
COG0131. LUCA.
HOGENOMiHOG000228064.
InParanoidiO23346.
KOiK01693.
PhylomeDBiO23346.

Family and domain databases

HAMAPiMF_00076. HisB.
InterProiIPR000807. ImidazoleglycerolP_deHydtase.
IPR020565. ImidazoleglycerP_deHydtase_CS.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamiPF00475. IGPD. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
PROSITEiPS00954. IGP_DEHYDRATASE_1. 1 hit.
PS00955. IGP_DEHYDRATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O23346-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MELLSSSPAQ LLRPNLSSRA LLPPRTSIAS SHPPPPRFLV MNSQSQHRPS
60 70 80 90 100
ISCASPPPGD NGFPAITTAS PIESARIGEV KRETKETNVS VKINLDGHGV
110 120 130 140 150
SDSSTGIPFL DHMLDQLASH GLFDVHVRAT GDTHIDDHHT NEDVALAIGT
160 170 180 190 200
ALLKALGERK GINRFGDFTA PLDEALIHVS LDLSGRPYLG YNLEIPTQRV
210 220 230 240 250
GTYDTQLVEH FFQSLVNTSG MTLHIRQLAG KNSHHIIEAT FKAFARALRQ
260 270
ATESDPRRGG TIPSSKGVLS RS
Length:272
Mass (Da):29,424
Last modified:September 22, 2009 - v2
Checksum:i1A2EA7E3D2A5B9B0
GO

Sequence cautioni

The sequence CAB10270.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB78533.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97337 Genomic DNA. Translation: CAB10270.1. Sequence problems.
AL161540 Genomic DNA. Translation: CAB78533.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE83520.1.
AY048237 mRNA. Translation: AAK82500.1.
AY094021 mRNA. Translation: AAM16177.1.
PIRiD71412.
RefSeqiNP_567448.1. NM_117577.3. [O23346-1]
UniGeneiAt.4308.

Genome annotation databases

EnsemblPlantsiAT4G14910.1; AT4G14910.1; AT4G14910. [O23346-1]
GeneIDi827149.
KEGGiath:AT4G14910.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97337 Genomic DNA. Translation: CAB10270.1. Sequence problems.
AL161540 Genomic DNA. Translation: CAB78533.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE83520.1.
AY048237 mRNA. Translation: AAK82500.1.
AY094021 mRNA. Translation: AAM16177.1.
PIRiD71412.
RefSeqiNP_567448.1. NM_117577.3. [O23346-1]
UniGeneiAt.4308.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MU0X-ray1.30A69-272[»]
4MU1X-ray1.50A54-272[»]
4MU3X-ray1.12A69-272[»]
4MU4X-ray1.41A69-272[»]
4QNJX-ray1.30A69-272[»]
4QNKX-ray1.75A/B/C/D/E/F/G/H70-272[»]
ProteinModelPortaliO23346.
SMRiO23346. Positions 74-258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi12446. 1 interaction.
DIPiDIP-61567N.
STRINGi3702.AT4G14910.2.

Proteomic databases

PaxDbiO23346.
PRIDEiO23346.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G14910.1; AT4G14910.1; AT4G14910. [O23346-1]
GeneIDi827149.
KEGGiath:AT4G14910.

Organism-specific databases

TAIRiAT4G14910.

Phylogenomic databases

eggNOGiKOG3143. Eukaryota.
COG0131. LUCA.
HOGENOMiHOG000228064.
InParanoidiO23346.
KOiK01693.
PhylomeDBiO23346.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00011.
BioCyciARA:GQT-1999-MONOMER.
ARA:GQT-2000-MONOMER.

Miscellaneous databases

PROiO23346.

Gene expression databases

ExpressionAtlasiO23346. baseline and differential.
GenevisibleiO23346. AT.

Family and domain databases

HAMAPiMF_00076. HisB.
InterProiIPR000807. ImidazoleglycerolP_deHydtase.
IPR020565. ImidazoleglycerP_deHydtase_CS.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamiPF00475. IGPD. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 2 hits.
PROSITEiPS00954. IGP_DEHYDRATASE_1. 1 hit.
PS00955. IGP_DEHYDRATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
    Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.
    , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
    Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. Cited for: GENE FAMILY, NOMENCLATURE.
  6. "Genetic dissection of histidine biosynthesis in Arabidopsis."
    Muralla R., Sweeney C., Stepansky A., Leustek T., Meinke D.
    Plant Physiol. 144:890-903(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.

Entry informationi

Entry nameiHIS5B_ARATH
AccessioniPrimary (citable) accession number: O23346
Secondary accession number(s): Q94AE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: September 22, 2009
Last modified: June 8, 2016
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.