A3Q127 (HIS4_MYCSJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoribosyl isomerase A

Alternative name(s):
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase
EC=5.3.1.16
N-(5'-phosphoribosyl)anthranilate isomerase
Short name=PRAI
EC=5.3.1.24
Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase

Gene names

Name:	priA
Synonyms:	hisA
Ordered Locus Names:	Mjls_3075

Organism

Mycobacterium sp. (strain JLS) [Complete proteome] [HAMAP]

Taxonomic identifier

164757 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in both the histidine and tryptophan biosynthetic pathways By similarity. HAMAP-Rule MF_01014
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-Rule MF_01014 N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP-Rule MF_01014
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. HAMAP-Rule MF_01014 Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP-Rule MF_01014
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the HisA/HisF family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Histidine biosynthesis Tryptophan 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 tryptophan 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 phosphoribosylanthranilate 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 – 248	248	Phosphoribosyl isomerase A HAMAP-Rule MF_01014		PRO_0000290566
Sites
	Active site	14	1	Proton acceptor By similarity
	Active site	133	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3Q127 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: 1A2CBB2F54221470	FASTA	248	26,204
	10 20 30 40 50 60 MSEKRPLILL PAVDVVEGRA VRLVQGKAGS ETEYGSALDA ALGWQRDGAE WIHLVDLDAA 70 80 90 100 110 120 FGRGSNRELL ADVVGRLDVA VELSGGIRDD ESLEAALATG CARVNIGTAA LENPQWCAKV 130 140 150 160 170 180 VAEFGDKVAV GLDVKIVDDQ HRLRGRGWET DGGDLWEVLD RLDSEGCSRY VVTDVTKDGT 190 200 210 220 230 240 LQGPNLDLLG RVADRTDAPV IASGGVSSLD DLRAIATLTD RGVEGAIVGK ALYAGRFTLP EALAAMGQ

References

[1]

"Complete sequence of Mycobacterium sp. JLS." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J., Sims R.C., Richardson P. Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JLS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000580 Genomic DNA. Translation: ABN98854.1.
RefSeq	YP_001071345.1. NC_009077.1.
3D structure databases
ProteinModelPortal	A3Q127.
SMR	A3Q127. Positions 7-245.
ModBase	Search...
Protein-protein interaction databases
STRING	164757.Mjls_3075.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABN98854; ABN98854; Mjls_3075.
GeneID	4878788.
KEGG	mjl:Mjls_3075.
PATRIC	18092333. VBIMycSp51234_3096.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0106.
HOGENOM	HOG000224614.
KO	K01814. K01817.
OMA	CARYVVT.
ProtClustDB	PRK14024.
Enzyme and pathway databases
BioCyc	MSP164757:GHV3-3128-MONOMER.
UniPathway	UPA00031; UER00009. UPA00035; UER00042.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01014. HisA.
InterPro	IPR013785. Aldolase_TIM. IPR006062. His_biosynth. IPR010188. HisA_TrpF. IPR023016. Isoase_HisA. IPR011060. RibuloseP-bd_barrel. [Graphical view]
Pfam	PF00977. His_biosynth. 1 hit. [Graphical view]
SUPFAM	SSF51366. RibP_bind_barrel. 1 hit.
TIGRFAMs	TIGR01919. hisA-trpF. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HIS4_MYCSJ

Accession

Primary (citable) accession number: A3Q127

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 12, 2007
Last sequence update:	April 3, 2007
Last modified:	May 1, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program