Reviewed, UniProtKB/Swiss-Prot Q3JN01 (HIS4_BURP1)

Names and origin

Protein names

Recommended name:
    1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase
    EC=5.3.1.16
Alternative name(s):
    Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase

Gene names

Name:	hisA
Ordered Locus Names:	BURPS1710b_3688

Organism

Burkholderia pseudomallei (strain 1710b) [Complete proteome] [HAMAP]

Taxonomic identifier

320372 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	251 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1-deoxyribulos-1-ylamino)methylideneamino)-1-(5-phosphoribosyl)imidazole-4-carboxamide. HAMAP MF_01014
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. HAMAP MF_01014
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the hisA/hisF family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Molecular function	Isomerase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 251	251	1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase HAMAP MF_01014		PRO_0000229046
Sites
	Active site	8	1	Proton acceptor By similarity
	Active site	131	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3JN01-1 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: D4699D04E831232F	FASTA	251	26,588
	10 20 30 40 50 60 MLLIPAIDLK DGQCVRLKQG DMDQATIFSE DPAAMARKWV DLGARRLHLV DLNGAFAGKP 70 80 90 100 110 120 KNLEAIEAIL GEVGDEIPVQ LGGGIRSLET IEKYLDAGLS YVIIGTAAVK DPGFLQDACS 130 140 150 160 170 180 AFAGNIIVGL DAKDGKVATD GWSKLTGHEV IDLARKFEDY GVESIVYTDI GRDGMLQGIN 190 200 210 220 230 240 IEATVKLAQA VGIPVIASGG LSNIVDIEKL CEVEDEGIEG VICGRAIYSG DLDFAAAQKR 250 ADELNGELDD A

References

[1]	Woods D.E., Nierman W.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000124 Genomic DNA. Translation: ABA48864.1.
RefSeq	YP_335052.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3690072.
GenomeReviews	Gene locus BURPS1710b_3688 in contig CP000124_GR.
KEGG	bpm:BURPS1710b_3688.
TIGR	BURPS1710b_3688.
Phylogenomic databases
HOGENOM	Q3JN01.
OMA	Q3JN01. VATRGWL.
Enzyme and pathway databases
BioCyc	BPSE320372:BURPS1710B_A3986-MON.
Family and domain databases
HAMAP	MF_01014. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR006063. His4. IPR006062. His_biosynth. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF00977. His_biosynth. 1 hit. [Graphical view]
TIGRFAMs	TIGR00007. His4. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HIS4_BURP1

Accession

Primary (citable) accession number: Q3JN01

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	November 8, 2005
Last modified:	June 16, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)