Reviewed, UniProtKB/Swiss-Prot A0KF84 (HUTI_AERHH)

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:	AHA_0377

Organism

Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]

Taxonomic identifier

380703 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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	3D-structure 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: HAMAP iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW zinc 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_0000306422

Sites

Metal binding

75

1

Zinc or iron HAMAP MF_00372

Metal binding

77

1

Zinc or iron HAMAP MF_00372

Metal binding

245

1

Zinc or iron HAMAP MF_00372

Metal binding

320

1

Zinc or iron HAMAP MF_00372

Binding site

84

1

Substrate HAMAP MF_00372

Binding site

97

1

Substrate By similarity

Binding site

147

1

Substrate HAMAP MF_00372

Binding site

180

1

Substrate HAMAP MF_00372

Binding site

248

1

Substrate HAMAP MF_00372

Secondary structure

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411

Helix Strand Turn

Details...

Beta strand

8 – 18

11

Beta strand

31 – 38

8

Beta strand

41 – 47

7

Helix

48 – 50

3

Beta strand

57 – 61

5

Beta strand

66 – 69

4

Beta strand

71 – 76

6

Helix

85 – 93

9

Helix

97 – 102

6

Helix

107 – 116

10

Helix

119 – 135

17

Beta strand

138 – 144

7

Helix

151 – 167

17

Beta strand

170 – 179

10

Helix

184 – 186

3

Helix

190 – 199

10

Helix

201 – 207

7

Beta strand

212 – 219

8

Helix

225 – 237

13

Beta strand

241 – 249

9

Helix

254 – 260

7

Beta strand

264 – 268

5

Helix

274 – 283

10

Beta strand

286 – 289

4

Helix

291 – 296

6

Helix

305 – 310

6

Beta strand

315 – 317

3

Turn

323 – 325

3

Helix

331 – 342

12

Helix

346 – 352

7

Helix

355 – 360

6

Turn

364 – 366

3

Beta strand

367 – 369

3

Beta strand

378 – 384

7

Helix

388 – 391

4

Beta strand

392 – 394

3

Beta strand

398 – 403

6

Sequences

	Sequence		Length	Mass (Da)
	A0KF84-1 [UniParc]. Last modified October 2, 2007. Version 2. Checksum: 63D38DB562DC8EBF	FASTA	411	44,543
	10 20 30 40 50 60 MNKELLNCER VWLNVTPATL RSDLADYGLL EPHALGVHEG RIHALVPMQD LKGPYPAHWQ 70 80 90 100 110 120 DMKGKLVTPG LIDCHTHLIF AGSRAEEFEL RQKGVPYAEI ARKGGGIIST VRATRAACEE 130 140 150 160 170 180 QLFELALPRV KSLIREGVTT VEIKSGYGLT LEDELKMLRV ARRLGEALPI RVKTTLLAAH 190 200 210 220 230 240 AVPPEYRDDP DSWVETICQE IIPAAAEAGL ADAVDVFCEH IGFSLAQTEQ VYLAADQYGL 250 260 270 280 290 300 AVKGHMDQLS NLGGSTLAAN FGALSVDHLE YLDPEGIQAL AHRGVVATLL PTAFYFLKET 310 320 330 340 350 360 KLPPVAALRK AGVPMAVSSD INPGTAPIVS LRMAMNMACT LFGLTPVEAM AGVTRHAARA 370 380 390 400 410 LGEQEQLGQL RVGMLADFLV WNCGHPAELS YLIGVDQLVS RVINGEETLH G

References

[1]

"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades." Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F. J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000462 Genomic DNA. Translation: ABK39901.1. Different initiation.

RefSeq

YP_854906.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OOF	X-ray	2.20	A	6-411	[»]
2Q09	X-ray	1.97	A	6-411	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

A0KF84.

Genome annotation databases

GeneID

4486961.

GenomeReviews

Gene locus AHA_0377 in contig CP000462_GR.

KEGG

aha:AHA_0377.

TIGR

AHA_0377.

Phylogenomic databases

eggNOG

COG1228.

HOGENOM

HBG686142.

Family and domain databases

HAMAP

MF_00372. HutI.
[Tree]

InterPro

IPR013108. Amidohydro_3.
IPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]

Pfam

PF07969. Amidohydro_3. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01224. hutI. 1 hit.

ProtoNet

Search...

Entry information

Entry name

HUTI_AERHH

Accession

Primary (citable) accession number: A0KF84

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	October 2, 2007
Last modified:	February 9, 2010
This is version 23 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)