P60579 (HIS4_MYCBO) 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:	Mb1629

Organism

Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]

Taxonomic identifier

233413 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium bovis

Protein attributes

Sequence length	244 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.
Sequence caution	The sequence CAD96297.1 differs from that shown. Reason: Erroneous initiation.

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 – 244	244	Phosphoribosyl isomerase A HAMAP-Rule MF_01014		PRO_0000142082
Sites
	Active site	10	1	Proton acceptor By similarity
	Active site	129	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P60579 [UniParc]. Last modified March 15, 2004. Version 1. Checksum: 8B9C2C403958A01E	FASTA	244	25,632
	10 20 30 40 50 60 MPLILLPAVD VVEGRAVRLV QGKAGSQTEY GSAVDAALGW QRDGAEWIHL VDLDAAFGRG 70 80 90 100 110 120 SNHELLAEVV GKLDVQVELS GGIRDDESLA AALATGCARV NVGTAALENP QWCARVIGEH 130 140 150 160 170 180 GDQVAVGLDV QIIDGEHRLR GRGWETDGGD LWDVLERLDS EGCSRFVVTD ITKDGTLGGP 190 200 210 220 230 240 NLDLLAGVAD RTDAPVIASG GVSSLDDLRA IATLTHRGVE GAIVGKALYA RRFTLPQALA AVRD

References

[1]

"The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G. Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248339 Genomic DNA. Translation: CAD96297.1. Different initiation.
RefSeq	NP_855282.1. NC_002945.3.
3D structure databases
ProteinModelPortal	P60579.
SMR	P60579. Positions 1-244.
ModBase	Search...
Protein-protein interaction databases
STRING	233413.Mb1629.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAD96297; CAD96297; Mb1629.
GeneID	1092522.
KEGG	mbo:Mb1629.
PATRIC	18005261. VBIMycBov88188_1778.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0106.
HOGENOM	HOG000224614.
KO	K01814. K01817.
OMA	CARYVVT.
ProtClustDB	PRK14024.
Enzyme and pathway databases
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_MYCBO

Accession

Primary (citable) accession number: P60579
Secondary accession number(s): O06588

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	March 15, 2004
Last modified:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program