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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi75 – 751Zinc or iron
Metal bindingi77 – 771Zinc or iron
Binding sitei84 – 841Substrate
Binding sitei97 – 971SubstrateUniRule annotation
Binding sitei147 – 1471Substrate
Binding sitei180 – 1801Substrate
Metal bindingi245 – 2451Zinc or iron
Binding sitei248 – 2481Substrate
Metal bindingi320 – 3201Zinc or iron

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

BioCyciAHYD380703:GH2M-378-MONOMER.
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411ImidazolonepropionasePRO_0000306422Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi380703.AHA_0377.

Structurei

Secondary structure

1
411
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 1810Combined sources
Beta strandi31 – 388Combined sources
Beta strandi41 – 477Combined sources
Helixi48 – 503Combined sources
Beta strandi59 – 613Combined sources
Beta strandi66 – 694Combined sources
Beta strandi71 – 766Combined sources
Helixi85 – 928Combined sources
Helixi97 – 1026Combined sources
Helixi107 – 11610Combined sources
Helixi119 – 13517Combined sources
Beta strandi138 – 1447Combined sources
Helixi151 – 16717Combined sources
Beta strandi168 – 17912Combined sources
Helixi184 – 1863Combined sources
Helixi190 – 19910Combined sources
Helixi201 – 2077Combined sources
Beta strandi212 – 2198Combined sources
Helixi225 – 23713Combined sources
Beta strandi241 – 2499Combined sources
Helixi254 – 2607Combined sources
Beta strandi264 – 2685Combined sources
Helixi274 – 28310Combined sources
Beta strandi286 – 2894Combined sources
Helixi291 – 2966Combined sources
Helixi305 – 3106Combined sources
Beta strandi315 – 3173Combined sources
Turni323 – 3253Combined sources
Helixi331 – 34212Combined sources
Helixi346 – 3527Combined sources
Helixi355 – 3606Combined sources
Turni364 – 3663Combined sources
Beta strandi367 – 3693Combined sources
Beta strandi378 – 3847Combined sources
Helixi388 – 3914Combined sources
Beta strandi398 – 4036Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OOFX-ray2.20A6-411[»]
2Q09X-ray1.97A6-411[»]
ProteinModelPortaliA0KF84.
SMRiA0KF84. Positions 6-410.
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.
RefSeqiWP_011704353.1. NC_008570.1.
YP_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.
RefSeqiWP_011704353.1. NC_008570.1.
YP_854906.1. NC_008570.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OOFX-ray2.20A6-411[»]
2Q09X-ray1.97A6-411[»]
ProteinModelPortaliA0KF84.
SMRiA0KF84. Positions 6-410.
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.
BioCyciAHYD380703:GH2M-378-MONOMER.

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: September 7, 2016
This is version 68 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.