P34047 (HIS7A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Imidazoleglycerol-phosphate dehydratase 1
Short name=IGPD 1
EC=4.2.1.19

Gene names

Ordered Locus Names:	At3g22425
ORF Names:	MCB17.17

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O.
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Sequence similarities	Belongs to the imidazoleglycerol-phosphate dehydratase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Coding sequence diversity	Alternative splicing
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histidine biosynthetic process Inferred from direct assay Ref.1. Source: TAIR
Molecular_function	imidazoleglycerol-phosphate dehydratase activity Inferred from direct assay Ref.1. Source: TAIR
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: P34047-1)

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.

Isoform 2 (identifier: P34047-2)

The sequence of this isoform differs from the canonical sequence as follows:
     205-270: LVEHFFQSLV...PSSKGVLSRS → VLSLLLELSS...YDSSHPAARW

Note: May be due to an intron retention.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 270

270

Imidazoleglycerol-phosphate dehydratase 1

PRO_0000158253

Natural variations

Alternative sequence

205 – 270

66

LVEHF…VLSRS → VLSLLLELSSFGFICVIRCL VIIESVAKNCLTFRFVVGGA LFPVVGEYFWYDSSHPAARW in isoform 2.

VSP_008895

Secondary structure

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270

Helix Strand Turn

Details...

Beta strand

75 – 81

7

Beta strand

86 – 92

7

Beta strand

99 – 102

4

Helix

106 – 119

14

Beta strand

122 – 128

7

Turn

131 – 133

3

Helix

136 – 154

19

Beta strand

166 – 170

5

Beta strand

173 – 180

8

Beta strand

186 – 190

5

Beta strand

194 – 198

5

Helix

205 – 217

13

Beta strand

220 – 227

8

Helix

231 – 250

20

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 7132D80CC687E20C	FASTA	270	29,225
	10 20 30 40 50 60 MELSSASAIL SHSSSAAQLL RPKLGFIDLL PRRAMIVSSP SSSLPRFLRM ESQSQLRQSI 70 80 90 100 110 120 SCSASSSSSM ALGRIGEVKR VTKETNVSVK INLDGTGVAD SSSGIPFLDH MLDQLASHGL 130 140 150 160 170 180 FDVHVRATGD VHIDDHHTNE DIALAIGTAL LKALGERKGI NRFGDFTAPL DEALIHVSLD 190 200 210 220 230 240 LSGRPYLGYN LEIPTQRVGT YDTQLVEHFF QSLVNTSGMT LHIRQLAGEN SHHIIEATFK 250 260 270 AFARALRQAT ETDPRRGGTI PSSKGVLSRS
	Isoform 2 [UniParc]. Checksum: 8551F5DED1EB8CAD	FASTA	264	28,691
	10 20 30 40 50 60 MELSSASAIL SHSSSAAQLL RPKLGFIDLL PRRAMIVSSP SSSLPRFLRM ESQSQLRQSI 70 80 90 100 110 120 SCSASSSSSM ALGRIGEVKR VTKETNVSVK INLDGTGVAD SSSGIPFLDH MLDQLASHGL 130 140 150 160 170 180 FDVHVRATGD VHIDDHHTNE DIALAIGTAL LKALGERKGI NRFGDFTAPL DEALIHVSLD 190 200 210 220 230 240 LSGRPYLGYN LEIPTQRVGT YDTQVLSLLL ELSSFGFICV IRCLVIIESV AKNCLTFRFV 250 260 VGGALFPVVG EYFWYDSSHP AARW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of cDNAs encoding imidazoleglycerolphosphate dehydratase from Arabidopsis thaliana." Tada S., Volrath S., Guyer D., Scheidegger A., Ryals J., Ohta D., Ward E. Plant Physiol. 105:579-583(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S. DNA Res. 7:131-135(2000) [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]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: cv. Columbia.
[5]	"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] (ISOFORM 2). Strain: cv. Columbia.
[6]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: cv. Columbia.
[7]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U02689 mRNA. Translation: AAA93196.1.
AB022215 Genomic DNA. Translation: BAB01781.1.
CP002686 Genomic DNA. Translation: AEE76636.1.
CP002686 Genomic DNA. Translation: AEE76637.1.
AK118815 mRNA. Translation: BAC43405.1.
AY070442 mRNA. Translation: AAL49845.1.
AK176429 mRNA. Translation: BAD44192.1.
AY087948 mRNA. Translation: AAM65496.1.

IPI

IPI00523383.
IPI00541298.

RefSeq

NP_850624.1. NM_180293.1.
NP_850625.1. NM_180294.1.

UniGene

At.19962.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F1D	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P	64-270	[»]

ProteinModelPortal

P34047.

SMR

P34047. Positions 73-255.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48462N.

Proteomic databases

PaxDb

P34047.

PRIDE

P34047.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

AT3G22425.2; AT3G22425.2; AT3G22425.

GeneID

821812.

KEGG

ath:AT3G22425.

Organism-specific databases

TAIR

At3g22425.

Phylogenomic databases

eggNOG

COG0131.

HOGENOM

HOG000228064.

InParanoid

P34047.

KO

K01693.

OMA

HHIVEAC.

PhylomeDB

P34047.

ProtClustDB

PLN02800.

Enzyme and pathway databases

UniPathway

UPA00031; UER00011.

Gene expression databases

ArrayExpress

P34047.

Genevestigator

P34047.

GermOnline

AT3G22425. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR000807. ImidazoleglycerolP_deHydtase.
IPR020565. ImidazoleglycerP_deHydtase_CS.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]

PANTHER

PTHR23133:SF2. PTHR23133:SF2. 1 hit.

Pfam

PF00475. IGPD. 1 hit.
[Graphical view]

SUPFAM

SSF54211. Ribosomal_S5_D2-typ_fold. 2 hits.

PROSITE

PS00954. IGP_DEHYDRATASE_1. 1 hit.
PS00955. IGP_DEHYDRATASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P34047.

Entry information

Entry name

HIS7A_ARATH

Accession

Primary (citable) accession number: P34047
Secondary accession number(s): Q67YN9, Q8VYM1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program