A0LZE0 (HUTI_GRAFK) 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:	GFO_0758

Organism

Gramella forsetii (strain KT0803) [Complete proteome] [HAMAP]

Taxonomic identifier

411154 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Gramella

Protein attributes

Sequence length	411 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 – 411	411	Imidazolonepropionase HAMAP MF_00372		PRO_0000306464
Sites
	Metal binding	78	1	Zinc or iron By similarity
	Metal binding	80	1	Zinc or iron By similarity
	Metal binding	248	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	251	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0LZE0 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: 798349CC3C8A97F0	FASTA	411	45,460
	10 20 30 40 50 60 MTLLVTNIKE LLQVREQNIL KVSGSEMKEL PTIKNAWLLI ENDKIADFGT MKNMPKITAD 70 80 90 100 110 120 QTIDATGKIV LPTWCDSHTH IVYAGNREQE FADRINGLSY EEIANRGGGI LNSVKTLQDT 130 140 150 160 170 180 SEEEVYEQSA KRLKEVMKLG TGAVEIKSGY GLTEKAELKM LRVIKKLREN YDLPVKSTFL 190 200 210 220 230 240 GAHAIPKEYK NDPDAYMDLV INEILPKVAK EGLAEYIDIF CEKGYFSIKD THRLLSAAKE 250 260 270 280 290 300 HGLKPKIHVN QFNSIGGVKV GVEHEALSVD HLEVMNDEDI EVLKGTRTMP VALPSCSLFL 310 320 330 340 350 360 SIPYTPARKI LDAELPLALA TDFNPGSTPS GNMNLVVSLA CIKMKMTPEE AINAATINGA 370 380 390 400 410 YAMDLSETHG SITKGKMANF MITKEIPSFT FLPYAFGTNS IDSVYINGKL I

References

[1]

"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter." Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O. Environ. Microbiol. 8:2201-2213(2006) [PubMed: 17107561] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KT0803.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU207366 Genomic DNA. Translation: CAL65735.1.
RefSeq	YP_860802.1. NC_008571.1.
3D structure databases
ProteinModelPortal	A0LZE0.
ModBase	Search...
Protein-protein interaction databases
STRING	A0LZE0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4652556.
GenomeReviews	Gene locus GFO_0758 in contig CU207366_GR.
KEGG	gfo:GFO_0758.
NMPDR	fig|411154.5.peg.722.
PATRIC	22070367. VBIGraFor5527_0733.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1228.
HOGENOM	HBG686142.
OMA	MNMACTL.
ProtClustDB	PRK09356.
Enzyme and pathway databases
BioCyc	GFOR411154:GFO_0758-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_GRAFK

Accession

Primary (citable) accession number: A0LZE0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	December 12, 2006
Last modified:	January 25, 2012
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program