A0RH37 (HUTI_BACAH) 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:	BALH_3285

Organism

Bacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP]

Taxonomic identifier

412694 [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_0000306433
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)
	A0RH37 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: ABD5333BEAFF34BD	FASTA	423	46,185
	10 20 30 40 50 60 MLDTLLINIG QLLTMDQEDG LLRREAMNTL PVIENGAVGI ENGVITFVGT AEEAKGLQAK 70 80 90 100 110 120 EVIDCGGKMV SPGLVDPHTH LVFGGSRENE IALKLQGVPY LEILEQGGGI LSTVNATKQA 130 140 150 160 170 180 SKEELVQKAK FHLDRMLSFG VTTVEAKSGY GLDDETEWKQ LEATAQLQKE HPIDLVSTFL 190 200 210 220 230 240 GAHAVPKEYK GRSKEFLQWM LDLLPEMKEK QLAEFVDIFC ETGVFSVEES KEFLLKAKEL 250 260 270 280 290 300 GFDVKIHADE IDPLGGAEAA AEIGAASADH LVGASDKGIE MLANSNTVAT LLPGTTFYLN 310 320 330 340 350 360 KESFARGRKM IDEGVAVALA TDFNPGSCPT ENIQLIMSIA MLKLKMTPEE VWNAVTVNSS 370 380 390 400 410 420 YAINRGEVAG KIRVGRKADL VLWDAYNYAY VPYHYGVSHV NTVWKNGNIA YTRGEQSWST ATI

References

[1]

"The complete genome sequence of Bacillus thuringiensis Al Hakam." Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Green L.D., Han C.S. , Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S. J. Bacteriol. 189:3680-3681(2007) [PubMed: 17337577] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Al Hakam.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000485 Genomic DNA. Translation: ABK86530.1.
RefSeq	YP_896037.1. NC_008600.1.
3D structure databases
ProteinModelPortal	A0RH37.
SMR	A0RH37. Positions 2-413.
ModBase	Search...
Protein-protein interaction databases
STRING	A0RH37.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000070681; EBBACP00000068918; EBBACG00000070672.
GeneID	4544489.
GenomeReviews	Gene locus BALH_3285 in contig CP000485_GR.
KEGG	btl:BALH_3285.
NMPDR	fig|412694.5.peg.3151.
PATRIC	18999305. VBIBacThu63319_3652.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1228.
GeneTree	EBGT00050000002251.
HOGENOM	HBG686142.
OMA	MNMACTL.
ProtClustDB	PRK09356.
Enzyme and pathway databases
BioCyc	BTHU412694:BALH_3285-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_BACAH

Accession

Primary (citable) accession number: A0RH37

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	January 9, 2007
Last modified:	January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program