Reviewed, UniProtKB/Swiss-Prot Q7TV28 (HIS2_PROMM)

Names and origin

Protein names

Recommended name:
    Histidine biosynthesis bifunctional protein hisIE
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosyl-AMP cyclohydrolase
                Short name=PRA-CH
              EC=3.5.4.19
    2- Recommended name:
            Phosphoribosyl-ATP pyrophosphatase
                Short name=PRA-PH
              EC=3.6.1.31

Gene names

Name:	hisI
Synonyms:	hisIE
Ordered Locus Names:	PMT_0453

Organism

Prochlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]

Taxonomic identifier

74547 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	222 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)-ATP + H2O = 1-(5-phosphoribosyl)-AMP + diphosphate. HAMAP MF_01019 1-(5-phosphoribosyl)-AMP + H2O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. HAMAP MF_01019
Pathway	Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. HAMAP MF_01019 Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	In the N-terminal section; belongs to the PRA-CH family. In the C-terminal section; belongs to the PRA-PH family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Histidine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome Multifunctional enzyme
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	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoribosyl-AMP cyclohydrolase activity Inferred from electronic annotation. Source: HAMAP phosphoribosyl-ATP diphosphatase 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 – 222	222	Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019		PRO_0000136424
Regions
	Region	1 – 128	128	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	129 – 222	94	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	Q7TV28-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: F77F4AFC2137219B	FASTA	222	24,827
	10 20 30 40 50 60 MQPLSPAFID QLCFDDIGLI PAISQDWLDG AVLMMAWMNR TALEQTLKSG QVHYWSRSRQ 70 80 90 100 110 120 ELWHKGATSG HTQILKGIRY DCDADVLLLS IEQTGLVSCH TGARSCFFAE VNQHSQGDSL 130 140 150 160 170 180 TLPPPMDACS ELFRVIDQRH TTPEANSYTN KLLEGGDNRI LKKIGEESAE FVMACKDDDE 190 200 210 220 KAIANEAADL LFHLQVALAH HGVNWRDVLE VLANRRGAPR RN

References

[1]

"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation." Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W. Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX548175 Genomic DNA. Translation: CAE20628.1.
RefSeq	NP_894286.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1729694.
GenomeReviews	Gene locus PMT_0453 in contig BX548175_GR.
KEGG	pmt:PMT0453.
NMPDR	fig|74547.1.peg.453.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7TV28.
OMA	Q7TV28. VHYWSRS.
Enzyme and pathway databases
BioCyc	PMAR74547:PMT0453-MON.
Family and domain databases
HAMAP	MF_01019. [Tree]
InterPro	IPR002496. PRA_CycHdrlase. IPR008179. PRib-ATP_pyrophosphohydrolase. [Graphical view]
Pfam	PF01502. PRA-CH. 1 hit. PF01503. PRA-PH. 1 hit. [Graphical view]
ProDom	PD002610. PRA_cyclohydro. 1 hit. PD002611. Pra_PH/CH. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03188. histidine_hisI. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HIS2_PROMM

Accession

Primary (citable) accession number: Q7TV28

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	October 1, 2003
Last modified:	June 16, 2009
This is version 36 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)