A7GQZ8 (HUTI_BACCN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Imidazolonepropionase
EC=3.5.2.7

Alternative name(s):
Imidazolone-5-propionate hydrolase

Gene names

Name:	hutI
Ordered Locus Names:	Bcer98_2310

Organism

Bacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]

Taxonomic identifier

315749 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O = N-formimidoyl-L-glutamate + H+. HAMAP MF_00372
Cofactor	Binds 1 zinc or iron ion per subunit By similarity. HAMAP MF_00372
Pathway	Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3. HAMAP MF_00372
Subcellular location	Cytoplasm Potential HAMAP MF_00372.
Sequence similarities	Belongs to the HutI family.

Ontologies

Keywords
Biological process	Histidine metabolism
Cellular component	Cytoplasm
Ligand	Iron Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	histidine catabolic process to glutamate and formamide Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	imidazolonepropionase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 423	423	Imidazolonepropionase HAMAP MF_00372		PRO_1000079819
Sites
	Metal binding	78	1	Zinc or iron By similarity
	Metal binding	80	1	Zinc or iron By similarity
	Metal binding	247	1	Zinc or iron By similarity
	Metal binding	322	1	Zinc or iron By similarity
	Binding site	87	1	Substrate By similarity
	Binding site	100	1	Substrate By similarity
	Binding site	150	1	Substrate By similarity
	Binding site	183	1	Substrate By similarity
	Binding site	250	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7GQZ8 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: 4321F7912C37D4C7	FASTA	423	46,102
	10 20 30 40 50 60 MLDILLTNIG QLLTMDQEDG VLRQEAMKTL PVIESGAVGI KDGVIMFVGT AEEAKGLQAR 70 80 90 100 110 120 EIIDCEGKVV SPGLVDPHTH LVFGGSRENE IALKLQGVPY LEILEQGGGI LSTVNATKKA 130 140 150 160 170 180 SKEELVKKAN FHLDRMLSFG VTTVEAKSGY GLDDETEWKQ LEVVAQLQKE HPIDLVSTFL 190 200 210 220 230 240 GAHAVPKEYK GKSKEFLQWM LDLLPAIKEK ELAEFVDIFC ETGVFSVEES KEFLLEAKEL 250 260 270 280 290 300 GFDVKIHADE IDPLGGAEAA AEIGAASADH LVGASDKGIE MLANSNTVAT LLPGTTFYLN 310 320 330 340 350 360 KESFARGRKM IDEGVAVALA TDFNPGSCPT ENIQLVMSIA MLKLKMTPEE VWNAVTVNSA 370 380 390 400 410 420 YAINRGDVAG KIRVGRKADL VLWDAHHYAY VPYHYGVSHV NTVWKNGNLA YTRGDKAWSK ATI

References

[1]

"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity." Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A. Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NVH 391-98.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000764 Genomic DNA. Translation: ABS22556.1.
RefSeq	YP_001375551.1. NC_009674.1.
3D structure databases
ProteinModelPortal	A7GQZ8.
SMR	A7GQZ8. Positions 2-413.
ModBase	Search...
Protein-protein interaction databases
STRING	A7GQZ8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000038852; EBBACP00000037903; EBBACG00000038843.
GeneID	5345660.
GenomeReviews	Gene locus Bcer98_2310 in contig CP000764_GR.
KEGG	bcy:Bcer98_2310.
PATRIC	18933210. VBIBacCyt128034_2449.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1228.
GeneTree	EBGT00050000002251.
HOGENOM	HBG686142.
OMA	MNMACTL.
ProtClustDB	PRK09356.
Enzyme and pathway databases
BioCyc	BCER315749:BCER98_2310-MONOMER.
Family and domain databases
HAMAP	MF_00372. HutI. [Tree]
InterPro	IPR006680. Amidohydro_1. IPR005920. HutI. IPR011059. Metal-dep_hydrolase_composite. [Graphical view]
KO	K01468.
PANTHER	PTHR22642. PTHR22642. 1 hit.
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
SUPFAM	SSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMs	TIGR01224. HutI. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HUTI_BACCN

Accession

Primary (citable) accession number: A7GQZ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	September 11, 2007
Last modified:	January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program