Q9KBE4 (HUTI_BACHD) 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:	BH1984

Organism

Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]

Taxonomic identifier

272558 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	426 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 – 426	426	Imidazolonepropionase HAMAP MF_00372		PRO_0000160943
Sites
	Metal binding	80	1	Zinc or iron By similarity
	Metal binding	82	1	Zinc or iron By similarity
	Metal binding	249	1	Zinc or iron By similarity
	Metal binding	324	1	Zinc or iron By similarity
	Binding site	89	1	Substrate By similarity
	Binding site	102	1	Substrate By similarity
	Binding site	152	1	Substrate By similarity
	Binding site	185	1	Substrate By similarity
	Binding site	252	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KBE4 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 9E51D1C58F3A8F81	FASTA	426	46,494
	10 20 30 40 50 60 MVQHFDTLLV NIGQLLPMES KGPKRGKEMS ELQLLEHAAL GIRDGKVAFI GTMVEADTFT 70 80 90 100 110 120 ANQMIDCQGK LVTPGLVDPH THLIFGGSRE HEMALKQQGV PYLEILKNGG GILATVEATR 130 140 150 160 170 180 AASEEELITK AICHLNRMLS YGVTTIEAKS GYGLDRETEW KQLRAAKAVG EQHPIDIVST 190 200 210 220 230 240 FLGAHAIPTS HRNDPDRFLD EMADMLGEIK EQNLAEFVDI FTETGVFTVE QSRTFLQKAK 250 260 270 280 290 300 ERGFGLKLHA DEIDPLGGAE LAGELGAISA DHLVGASDQG IQKMAAAGTI ACLLPGTTFY 310 320 330 340 350 360 LGKDTYARAR DMIDQGLAVT ISTDFNPGSS PTENLQLIMS IAALRLKMTP EEIWHAVTVN 370 380 390 400 410 420 GAHAIGRGDT AGQLAVGRAA DVVVWDAKNY YYVPYHYGVN HVHSVWKKGE VVYERRRAFE GLSISR

References

[1]

"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000004 Genomic DNA. Translation: BAB05703.1.
PIR	H83897.
RefSeq	NP_242850.1. NC_002570.2.
3D structure databases
ProteinModelPortal	Q9KBE4.
SMR	Q9KBE4. Positions 3-415.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000052918; EBBACP00000051557; EBBACG00000052909.
GeneID	892067.
GenomeReviews	Gene locus BH1984 in contig BA000004_GR.
KEGG	bha:BH1984.
NMPDR	fig|272558.1.peg.1984.
PATRIC	18941110. VBIBacHal18977_2068.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000002251.
HOGENOM	HBG686142.
OMA	MNMACTL.
ProtClustDB	PRK09356.
Enzyme and pathway databases
BioCyc	BHAL272558:BH1984-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_BACHD

Accession

Primary (citable) accession number: Q9KBE4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program