Q8FVB5 (HUTI_BRUSU) 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:	BRA0929, BS1330_II0921

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

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 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 – 405	405	Imidazolonepropionase HAMAP MF_00372		PRO_0000160945
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)
	Q8FVB5 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 1EBD677910919A98	FASTA	405	43,448
	10 20 30 40 50 60 MTKNSSTVFT HARIATLEEK AANLGLIEEA ALVVKDARIV YAGPENKLPG 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 DGDGAAAMAS 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]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014292 Genomic DNA. Translation: AAN34101.1. CP002998 Genomic DNA. Translation: AEM20377.1.
RefSeq	NP_700096.1. NC_004311.2.
3D structure databases
ProteinModelPortal	Q8FVB5.
SMR	Q8FVB5. Positions 5-404.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1165373.
GenomeReviews	Gene locus BRA0929 in contig AE014292_GR.
KEGG	bms:BRA0929.
NMPDR	fig|204722.1.peg.3005.
PATRIC	17794677. VBIBruSui107850_3147.
TIGR	BRA0929.
Phylogenomic databases
HOGENOM	HBG686142.
OMA	MNMACTL.
ProtClustDB	PRK09356.
Enzyme and pathway databases
BioCyc	BSUI204722:BR_A0929-MONOMER.
Family and domain databases
HAMAP	MF_00372. HutI. [Tree]
InterPro	IPR013108. Amidohydro_3. IPR005920. HutI. IPR011059. Metal-dep_hydrolase_composite. [Graphical view]
KO	K01468.
PANTHER	PTHR22642. PTHR22642. 1 hit.
Pfam	PF07969. Amidohydro_3. 1 hit. [Graphical view]
SUPFAM	SSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMs	TIGR01224. HutI. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HUTI_BRUSU

Accession

Primary (citable) accession number: Q8FVB5
Secondary accession number(s): G0KDT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program