A8MF65 (HUTI_ALKOO) 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:	Clos_1188

Organism

Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OhILAs)) [Complete proteome] [HAMAP]

Taxonomic identifier

350688 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Alkaliphilus

Protein attributes

Sequence length	422 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 – 422	422	Imidazolonepropionase HAMAP MF_00372		PRO_1000059942
Sites
	Metal binding	82	1	Zinc or iron By similarity
	Metal binding	84	1	Zinc or iron By similarity
	Metal binding	252	1	Zinc or iron By similarity
	Metal binding	327	1	Zinc or iron By similarity
	Binding site	91	1	Substrate By similarity
	Binding site	104	1	Substrate By similarity
	Binding site	154	1	Substrate By similarity
	Binding site	187	1	Substrate By similarity
	Binding site	255	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8MF65 [UniParc]. Last modified December 4, 2007. Version 1. Checksum: DE5043412735781B	FASTA	422	45,757
	10 20 30 40 50 60 MNIDVWIKNI TQLVTVQAHG KPKKGKEMQD VGIIQDGWIA VAGDRIVGIG SGEISADFQV 70 80 90 100 110 120 GENTVIISGE GKTVTPGLID PHTHLVHAGS RENELALKLK GVPYLEILKQ GGGILSTVNA 130 140 150 160 170 180 TKKATMEELV AQSKKSLDRM LSYGVTTVEI KSGYGLELEA EIKQLEAIHR LQQQTPMDLV 190 200 210 220 230 240 STFMGAHAIP KEYKENPEEF IDLIIEEMLP AIKEKNLAEF CDVFCEEGVF SVDQTRRILE 250 260 270 280 290 300 AARSLGFKNK IHADEIVPLG GAELAAELQT ISAEHLMAAS ETGLKMMAES NVVPVALPGT 310 320 330 340 350 360 SFNLATGKYA DARKMIEYGL PVALATDYNP GSCPTENIQL IMSIGCLYLK MTPEEVISAV 370 380 390 400 410 420 TINAAAAIDR TQEIGSIEVG KKADITIFDA PNLYYIPYHF GVNHVDTVLK SGKIVVEKGN VI

References

[1]

"Complete genome of Alkaliphilus oremlandii OhILAs." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: OhILAs.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000853 Genomic DNA. Translation: ABW18734.1.
RefSeq	YP_001512730.1. NC_009922.1.
3D structure databases
ProteinModelPortal	A8MF65.
SMR	A8MF65. Positions 7-418.
ModBase	Search...
Protein-protein interaction databases
STRING	A8MF65.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5676593.
GenomeReviews	Gene locus Clos_1188 in contig CP000853_GR.
KEGG	aoe:Clos_1188.
PATRIC	20867571. VBIAlkOre124042_1243.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG686142.
OMA	MNMACTL.
ProtClustDB	PRK09356.
Enzyme and pathway databases
BioCyc	AORE350688:CLOS_1188-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_ALKOO

Accession

Primary (citable) accession number: A8MF65

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	December 4, 2007
Last modified:	January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program