Q579E7 (HUTI_BRUAB) 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:	BruAb2_0304

Organism

Brucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]

Taxonomic identifier

262698 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella abortus › Brucella abortus bv. 1

Protein attributes

Sequence length	405 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-Rule MF_00372
Cofactor	Binds 1 zinc or iron ion per subunit By similarity.
Pathway	Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3. HAMAP-Rule MF_00372
Subcellular location	Cytoplasm Potential HAMAP-Rule 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: UniProtKB-UniPathway histidine catabolic process to glutamate and formate Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	imidazolonepropionase activity Inferred from electronic annotation. Source: HAMAP iron ion binding Inferred from electronic annotation. Source: HAMAP zinc ion binding 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 – 405	405	Imidazolonepropionase HAMAP-Rule MF_00372		PRO_0000306443
Sites
	Metal binding	73	1	Zinc or iron By similarity
	Metal binding	75	1	Zinc or iron By similarity
	Metal binding	243	1	Zinc or iron By similarity
	Metal binding	318	1	Zinc or iron By similarity
	Binding site	82	1	Substrate By similarity
	Binding site	95	1	Substrate By similarity
	Binding site	145	1	Substrate By similarity
	Binding site	178	1	Substrate By similarity
	Binding site	246	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q579E7 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: A55470DFB24E994E	FASTA	405	43,520
	10 20 30 40 50 60 MTKNSSTVFT HARIATLEEK AANLGLIEEA ALVVKDARIV YAGPENKLPD EYASFEKIDC 70 80 90 100 110 120 GNRLITPGLI DCHTHLVHAG NRAHEFELRL QGATYEEVAR AGGGIVSSVR NLRAASEDDL 130 140 150 160 170 180 VRETLPRLDA LIAEGVTTVE VKSGYGLDRD SEIKSLKAAR RLGEERDVAI RTTFLGAHAL 190 200 210 220 230 240 PPEMNGDKAA YIDRVINDML PAIAEQGLAD AVDGFCEGIA FLPDEIARVF DAAKAHDIPV 250 260 270 280 290 300 KLHADQLSNL HGAALAASYG ALSADHLEYT DADGAAAMAS AGTVAVLLPG AYYFIRETQK 310 320 330 340 350 360 PPVEAFRAAG TKMALATDNN PGTSPLTSLL LTMNMGATLF RMTVEECIAG VTREAARALG 370 380 390 400 ILDQTGTLEI GKDADLAIWD IERPAELVYR IGFNPLWKRV FKGQI

References

[1]

"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017224 Genomic DNA. Translation: AAX75737.1.
RefSeq	YP_223098.1. NC_006933.1.
3D structure databases
HSSP	HSSP built from PDB template 2GOK based on UniProtKB Q8U8Z6.
ProteinModelPortal	Q579E7.
SMR	Q579E7. Positions 5-404.
ModBase	Search...
Protein-protein interaction databases
STRING	262698.BruAb2_0304.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAX75737; AAX75737; BruAb2_0304.
GeneID	3341633.
KEGG	bmb:BruAb2_0304.
PATRIC	17826844. VBIBruAbo15061_2605.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1228.
HOGENOM	HOG000218461.
KO	K01468.
OMA	MNMACTL.
ProtClustDB	PRK09356.
Enzyme and pathway databases
BioCyc	BABO262698:GJC2-2513-MONOMER.
UniPathway	UPA00379; UER00551.
Family and domain databases
HAMAP	MF_00372. HutI.
InterPro	IPR005920. HutI. IPR011059. Metal-dep_hydrolase_composite. [Graphical view]
PANTHER	PTHR22642. PTHR22642. 1 hit.
SUPFAM	SSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMs	TIGR01224. hutI. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HUTI_BRUAB

Accession

Primary (citable) accession number: Q579E7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program