Reviewed, UniProtKB/Swiss-Prot Q7TUC7 (HIS2_PROMP)

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:	PMM0578

Organism

Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]

Taxonomic identifier

59919 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	221 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 – 221	221	Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019		PRO_0000136425
Regions
	Region	1 – 129	129	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	130 – 221	92	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	Q7TUC7-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: E7E3F7C964AE14C6	FASTA	221	25,197
	10 20 30 40 50 60 MAYSKNFSIE ELRFDNKGLI PAIAQDWLDG SILMLAWMNK ESLNKTLETR NVHYWSRSRS 70 80 90 100 110 120 EIWRKGATSG STQFLKEIRF DCDNDALVLS IEQNGSGACH TGEKSCFFNE IDSISMNKTA 130 140 150 160 170 180 KKTSPFSNIC SELFDTLHER SINPLEKSYT NHLLTKGSNT ILKKIGEETA EFIMACKDND 190 200 210 220 KDEIANEASD IIYHLQVALI YKGVKWRDVL NVLESRRGKN N

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	BX548174 Genomic DNA. Translation: CAE19037.1.
RefSeq	NP_892696.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1726317.
GenomeReviews	Gene locus PMM0578 in contig BX548174_GR.
KEGG	pmm:PMM0578.
NMPDR	fig|59919.1.peg.575.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7TUC7.
OMA	Q7TUC7. VHYWSRS.
Enzyme and pathway databases
BioCyc	PMAR167540:PMM0578-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_PROMP

Accession

Primary (citable) accession number: Q7TUC7

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)