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Protein

Imidazolonepropionase

Gene

hutI

Organism
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O = N-formimidoyl-L-glutamate + H+.UniRule annotation

Cofactori

Zn2+UniRule annotation, Fe2+UniRule annotationNote: Binds 1 zinc or iron ion per subunit.UniRule annotation

Pathwayi: L-histidine degradation into L-glutamate

This protein is involved in step 3 of the subpathway that synthesizes N-formimidoyl-L-glutamate from L-histidine.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Histidine ammonia-lyase (hutH)
  2. Urocanate hydratase (hutU)
  3. Imidazolonepropionase (hutI)
This subpathway is part of the pathway L-histidine degradation into L-glutamate, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-formimidoyl-L-glutamate from L-histidine, the pathway L-histidine degradation into L-glutamate and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi75Zinc or iron1
Metal bindingi77Zinc or iron1
Binding sitei84Substrate1
Binding sitei97SubstrateUniRule annotation1
Binding sitei147Substrate1
Binding sitei180Substrate1
Metal bindingi245Zinc or iron1
Binding sitei248Substrate1
Metal bindingi320Zinc or iron1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Histidine metabolism

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00379; UER00551.

Protein family/group databases

MEROPSiM38.980.

Names & Taxonomyi

Protein namesi
Recommended name:
ImidazolonepropionaseUniRule annotation (EC:3.5.2.7UniRule annotation)
Alternative name(s):
Imidazolone-5-propionate hydrolaseUniRule annotation
Gene namesi
Name:hutIUniRule annotation
Ordered Locus Names:AHA_0377
OrganismiAeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)
Taxonomic identifieri380703 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas
Proteomesi
  • UP000000756 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003064221 – 411ImidazolonepropionaseAdd BLAST411

Interactioni

Protein-protein interaction databases

STRINGi380703.AHA_0377.

Structurei

Secondary structure

1411
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 18Combined sources10
Beta strandi31 – 38Combined sources8
Beta strandi41 – 47Combined sources7
Helixi48 – 50Combined sources3
Beta strandi59 – 61Combined sources3
Beta strandi66 – 69Combined sources4
Beta strandi71 – 76Combined sources6
Helixi85 – 92Combined sources8
Helixi97 – 102Combined sources6
Helixi107 – 116Combined sources10
Helixi119 – 135Combined sources17
Beta strandi138 – 144Combined sources7
Helixi151 – 167Combined sources17
Beta strandi168 – 179Combined sources12
Helixi184 – 186Combined sources3
Helixi190 – 199Combined sources10
Helixi201 – 207Combined sources7
Beta strandi212 – 219Combined sources8
Helixi225 – 237Combined sources13
Beta strandi241 – 249Combined sources9
Helixi254 – 260Combined sources7
Beta strandi264 – 268Combined sources5
Helixi274 – 283Combined sources10
Beta strandi286 – 289Combined sources4
Helixi291 – 296Combined sources6
Helixi305 – 310Combined sources6
Beta strandi315 – 317Combined sources3
Turni323 – 325Combined sources3
Helixi331 – 342Combined sources12
Helixi346 – 352Combined sources7
Helixi355 – 360Combined sources6
Turni364 – 366Combined sources3
Beta strandi367 – 369Combined sources3
Beta strandi378 – 384Combined sources7
Helixi388 – 391Combined sources4
Beta strandi398 – 403Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OOFX-ray2.20A6-411[»]
2Q09X-ray1.97A6-411[»]
ProteinModelPortaliA0KF84.
SMRiA0KF84.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA0KF84.

Family & Domainsi

Sequence similaritiesi

Belongs to the HutI family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CI2. Bacteria.
COG1228. LUCA.
HOGENOMiHOG000218461.
KOiK01468.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
HAMAPiMF_00372. HutI. 1 hit.
InterProiIPR006680. Amidohydro-rel.
IPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR01224. hutI. 1 hit.

Sequencei

Sequence statusi: Complete.

A0KF84-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKELLNCER VWLNVTPATL RSDLADYGLL EPHALGVHEG RIHALVPMQD
60 70 80 90 100
LKGPYPAHWQ DMKGKLVTPG LIDCHTHLIF AGSRAEEFEL RQKGVPYAEI
110 120 130 140 150
ARKGGGIIST VRATRAACEE QLFELALPRV KSLIREGVTT VEIKSGYGLT
160 170 180 190 200
LEDELKMLRV ARRLGEALPI RVKTTLLAAH AVPPEYRDDP DSWVETICQE
210 220 230 240 250
IIPAAAEAGL ADAVDVFCEH IGFSLAQTEQ VYLAADQYGL AVKGHMDQLS
260 270 280 290 300
NLGGSTLAAN FGALSVDHLE YLDPEGIQAL AHRGVVATLL PTAFYFLKET
310 320 330 340 350
KLPPVAALRK AGVPMAVSSD INPGTAPIVS LRMAMNMACT LFGLTPVEAM
360 370 380 390 400
AGVTRHAARA LGEQEQLGQL RVGMLADFLV WNCGHPAELS YLIGVDQLVS
410
RVINGEETLH G
Length:411
Mass (Da):44,543
Last modified:October 2, 2007 - v2
Checksum:i63D38DB562DC8EBF
GO

Sequence cautioni

The sequence ABK39901 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000462 Genomic DNA. Translation: ABK39901.1. Different initiation.
RefSeqiYP_854906.1. NC_008570.1.

Genome annotation databases

EnsemblBacteriaiABK39901; ABK39901; AHA_0377.
GeneIDi4486961.
KEGGiaha:AHA_0377.
PATRICi20778238. VBIAerHyd135212_0364.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000462 Genomic DNA. Translation: ABK39901.1. Different initiation.
RefSeqiYP_854906.1. NC_008570.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OOFX-ray2.20A6-411[»]
2Q09X-ray1.97A6-411[»]
ProteinModelPortaliA0KF84.
SMRiA0KF84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi380703.AHA_0377.

Protein family/group databases

MEROPSiM38.980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK39901; ABK39901; AHA_0377.
GeneIDi4486961.
KEGGiaha:AHA_0377.
PATRICi20778238. VBIAerHyd135212_0364.

Phylogenomic databases

eggNOGiENOG4105CI2. Bacteria.
COG1228. LUCA.
HOGENOMiHOG000218461.
KOiK01468.

Enzyme and pathway databases

UniPathwayiUPA00379; UER00551.

Miscellaneous databases

EvolutionaryTraceiA0KF84.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
HAMAPiMF_00372. HutI. 1 hit.
InterProiIPR006680. Amidohydro-rel.
IPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR01224. hutI. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHUTI_AERHH
AccessioniPrimary (citable) accession number: A0KF84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: November 2, 2016
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.