O34912 (HIS2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histidine biosynthesis bifunctional protein HisIE

Including the following 2 domains:

1. Phosphoribosyl-AMP cyclohydrolase
   Short name=PRA-CH
   EC=3.5.4.19
2. Phosphoribosyl-ATP pyrophosphatase
   Short name=PRA-PH
   EC=3.6.1.31

Gene names

Name:	hisI
Synonyms:	hisIE
Ordered Locus Names:	BSU34860

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	209 AA.
Sequence status	Complete.
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 HAMAP MF_01019.
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 Reference proteome
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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: EC phosphoribosyl-ATP diphosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 209	209	Histidine biosynthesis bifunctional protein HisIE HAMAP MF_01019		PRO_0000136403
Regions
	Region	1 – 116	116	Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019
	Region	117 – 209	93	Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019

Sequences

	Sequence		Length	Mass (Da)
	O34912 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: DEA9EB1F6A790F45	FASTA	209	23,901
	10 20 30 40 50 60 MKQADELRFN EDGLIPAIVQ DAASKEVLTL AYMNKESYEK TLETKETWFY SRSRQALWHK 70 80 90 100 110 120 GETSGNTQAV KGIRYDCDQD ALLVLVEPSG PACHTGSYSC FTKEQTEEQA ADRFGIMNEL 130 140 150 160 170 180 ERVIAERQAE MPEGAYTTYL FREGVDKILK KVGEEASEVI IAAKNRDHEE LKWEAADLLY 190 200 HLLVLLREQS LPLDDVLDVL KKRHSEIEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the 300-304 chromosomal segment of Bacillus subtilis." Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF017113 Genomic DNA. Translation: AAC67300.1. AL009126 Genomic DNA. Translation: CAB15491.1.
PIR	E69641.
RefSeq	NP_391366.1. NC_000964.3.
3D structure databases
ProteinModelPortal	O34912.
SMR	O34912. Positions 4-109, 117-207.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000001247; EBBACP00000001247; EBBACG00000001245.
GeneID	936552.
GenomeReviews	Gene locus BSU34860 in contig AL009126_GR.
KEGG	bsu:BSU34860.
NMPDR	fig|224308.1.peg.3492.
PATRIC	18978978. VBIBacSub10457_3651.
Organism-specific databases
GenoList	BSU34860. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000000892.
HOGENOM	HBG294308.
OMA	VMACKDD.
PhylomeDB	O34912.
ProtClustDB	PRK02759.
Enzyme and pathway databases
BioCyc	BSUB:BSU34860-MONOMER.
Family and domain databases
HAMAP	MF_01019. HisIE. [Tree]
InterPro	IPR023019. His_synth_HisIE. IPR008179. PRib-ATP_PPHydrolase. IPR021130. PRib-ATP_PPHydrolase-like. IPR002496. PRib_AMP_CycHydrolase. [Graphical view]
KO	K11755.
Pfam	PF01502. PRA-CH. 1 hit. PF01503. PRA-PH. 1 hit. [Graphical view]
ProDom	PD002610. PRA_CycHdrlase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR03188. Histidine_hisI. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HIS2_BACSU

Accession

Primary (citable) accession number: O34912

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program