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Protein

Imidazolonepropionase

Gene

hutI

Organism
Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
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+, Fe2+Note: Binds 1 zinc or iron ion per subunit.

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 bindingi84Zinc or iron1
Metal bindingi86Zinc or iron1
Binding sitei93SubstrateUniRule annotation1
Binding sitei106SubstrateUniRule annotation1
Binding sitei156Substrate1
Binding sitei189SubstrateUniRule annotation1
Metal bindingi254Zinc or iron1
Binding sitei257SubstrateUniRule annotation1
Metal bindingi329Zinc 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

BioCyciAGRO:ATU3934-MONOMER.
BRENDAi3.5.2.7. 200.
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:Atu3934
ORF Names:AGR_L_1824
OrganismiAgrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Taxonomic identifieri176299 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex
Proteomesi
  • UP000000813 Componenti: Chromosome linear

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_00001609421 – 419ImidazolonepropionaseAdd BLAST419

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi176299.Atu3934.

Structurei

Secondary structure

1419
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 25Combined sources10
Beta strandi36 – 45Combined sources10
Beta strandi48 – 54Combined sources7
Helixi60 – 62Combined sources3
Beta strandi66 – 70Combined sources5
Beta strandi75 – 78Combined sources4
Beta strandi80 – 82Combined sources3
Helixi94 – 101Combined sources8
Helixi106 – 111Combined sources6
Helixi116 – 125Combined sources10
Helixi128 – 143Combined sources16
Turni144 – 146Combined sources3
Beta strandi147 – 153Combined sources7
Helixi160 – 173Combined sources14
Turni174 – 176Combined sources3
Beta strandi180 – 185Combined sources6
Helixi193 – 195Combined sources3
Helixi199 – 205Combined sources7
Helixi207 – 216Combined sources10
Beta strandi221 – 223Combined sources3
Beta strandi226 – 228Combined sources3
Helixi234 – 246Combined sources13
Beta strandi251 – 259Combined sources9
Helixi263 – 269Combined sources7
Beta strandi273 – 277Combined sources5
Helixi283 – 292Combined sources10
Beta strandi295 – 298Combined sources4
Helixi300 – 306Combined sources7
Helixi314 – 320Combined sources7
Beta strandi324 – 326Combined sources3
Beta strandi332 – 334Combined sources3
Helixi340 – 351Combined sources12
Helixi355 – 361Combined sources7
Helixi364 – 369Combined sources6
Turni373 – 375Combined sources3
Beta strandi376 – 378Combined sources3
Beta strandi387 – 390Combined sources4
Helixi397 – 400Combined sources4
Beta strandi407 – 412Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GOKX-ray1.87A/B2-419[»]
2PUZX-ray1.83A/B1-419[»]
ProteinModelPortaliQ8U8Z6.
SMRiQ8U8Z6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8U8Z6.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni331 – 333Substrate binding3

Sequence similaritiesi

Belongs to the HutI family.UniRule annotation

Phylogenomic databases

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

Family and domain databases

CDDicd01296. Imidazolone-5PH. 1 hit.
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.

Q8U8Z6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGNNSAKGT ATGNATALWR NAQLATLNPA MDGIGAVENA VIAVRNGRIA
60 70 80 90 100
FAGPESDLPD DLSTADETTD CGGRWITPAL IDCHTHLVFG GNRAMEFEMR
110 120 130 140 150
LNGATYEEIA KAGGGIVSSV RDTRALSDEV LVAQALPRLD TLLSEGVSTI
160 170 180 190 200
EIKSGYGLDI ETELKMLRVA RRLETLRPVR IVTSYLAAHA TPADYKGRNA
210 220 230 240 250
DYITDVVLPG LEKAHAEGLA DAVDGFCEGI AFSVKEIDRV FAAAQQRGLP
260 270 280 290 300
VKLHAEQLSN LGGAELAASY NALSADHLEY LDETGAKALA KAGTVAVLLP
310 320 330 340 350
GAFYALREKQ LPPVQALRDA GAEIALATDC NPGTSPLTSL LLTMNMGATL
360 370 380 390 400
FRMTVEECLT ATTRNAAKAL GLLAETGTLE AGKSADFAIW DIERPAELVY
410
RIGFNPLHAR IFKGQKVSP
Length:419
Mass (Da):44,400
Last modified:June 1, 2002 - v1
Checksum:i55D09461815693CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE007870 Genomic DNA. Translation: AAK89486.2.
PIRiAH3040.
D98245.
RefSeqiNP_356701.2. NC_003063.2.
WP_010973444.1. NC_003063.2.

Genome annotation databases

EnsemblBacteriaiAAK89486; AAK89486; Atu3934.
GeneIDi1135808.
KEGGiatu:Atu3934.
PATRICi20817300. VBIAgrTum91616_3757.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE007870 Genomic DNA. Translation: AAK89486.2.
PIRiAH3040.
D98245.
RefSeqiNP_356701.2. NC_003063.2.
WP_010973444.1. NC_003063.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GOKX-ray1.87A/B2-419[»]
2PUZX-ray1.83A/B1-419[»]
ProteinModelPortaliQ8U8Z6.
SMRiQ8U8Z6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi176299.Atu3934.

Protein family/group databases

MEROPSiM38.980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK89486; AAK89486; Atu3934.
GeneIDi1135808.
KEGGiatu:Atu3934.
PATRICi20817300. VBIAgrTum91616_3757.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00379; UER00551.
BioCyciAGRO:ATU3934-MONOMER.
BRENDAi3.5.2.7. 200.

Miscellaneous databases

EvolutionaryTraceiQ8U8Z6.

Family and domain databases

CDDicd01296. Imidazolone-5PH. 1 hit.
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_AGRFC
AccessioniPrimary (citable) accession number: Q8U8Z6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: June 1, 2002
Last modified: November 2, 2016
This is version 99 of the entry and version 1 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.