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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi84 – 841Zinc or iron
Metal bindingi86 – 861Zinc or iron
Binding sitei93 – 931SubstrateUniRule annotation
Binding sitei106 – 1061SubstrateUniRule annotation
Binding sitei156 – 1561Substrate
Binding sitei189 – 1891SubstrateUniRule annotation
Metal bindingi254 – 2541Zinc or iron
Binding sitei257 – 2571SubstrateUniRule annotation
Metal bindingi329 – 3291Zinc 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

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 419419ImidazolonepropionasePRO_0000160942Add
BLAST

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

STRINGi176299.Atu3934.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 2510Combined sources
Beta strandi36 – 4510Combined sources
Beta strandi48 – 547Combined sources
Helixi60 – 623Combined sources
Beta strandi66 – 705Combined sources
Beta strandi75 – 784Combined sources
Beta strandi80 – 823Combined sources
Helixi94 – 1018Combined sources
Helixi106 – 1116Combined sources
Helixi116 – 12510Combined sources
Helixi128 – 14316Combined sources
Turni144 – 1463Combined sources
Beta strandi147 – 1537Combined sources
Helixi160 – 17314Combined sources
Turni174 – 1763Combined sources
Beta strandi180 – 1856Combined sources
Helixi193 – 1953Combined sources
Helixi199 – 2057Combined sources
Helixi207 – 21610Combined sources
Beta strandi221 – 2233Combined sources
Beta strandi226 – 2283Combined sources
Helixi234 – 24613Combined sources
Beta strandi251 – 2599Combined sources
Helixi263 – 2697Combined sources
Beta strandi273 – 2775Combined sources
Helixi283 – 29210Combined sources
Beta strandi295 – 2984Combined sources
Helixi300 – 3067Combined sources
Helixi314 – 3207Combined sources
Beta strandi324 – 3263Combined sources
Beta strandi332 – 3343Combined sources
Helixi340 – 35112Combined sources
Helixi355 – 3617Combined sources
Helixi364 – 3696Combined sources
Turni373 – 3753Combined sources
Beta strandi376 – 3783Combined sources
Beta strandi387 – 3904Combined sources
Helixi397 – 4004Combined sources
Beta strandi407 – 4126Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GOKX-ray1.87A/B2-419[»]
2PUZX-ray1.83A/B1-419[»]
ProteinModelPortaliQ8U8Z6.
SMRiQ8U8Z6. Positions 15-418.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8U8Z6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni331 – 3333Substrate binding

Sequence similaritiesi

Belongs to the HutI family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CI2. Bacteria.
COG1228. LUCA.
HOGENOMiHOG000218461.
KOiK01468.
OrthoDBiEOG63C0XD.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
HAMAPiMF_00372. HutI.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
2GOKX-ray1.87A/B2-419[»]
2PUZX-ray1.83A/B1-419[»]
ProteinModelPortaliQ8U8Z6.
SMRiQ8U8Z6. Positions 15-418.
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.
OrthoDBiEOG63C0XD.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ8U8Z6.

Family and domain databases

Gene3Di2.30.40.10. 2 hits.
HAMAPiMF_00372. HutI.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C58 / ATCC 33970.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C58 / ATCC 33970.
  3. "X-ray structure of imidazolonepropionase from Agrobacterium tumefaciens at 1.87 A resolution."
    Tyagi R., Kumaran D., Burley S.K., Swaminathan S.
    Proteins 69:652-658(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH PRODUCT AND IRON IONS, SUBUNIT.
  4. "A common catalytic mechanism for proteins of the HutI family."
    Tyagi R., Eswaramoorthy S., Burley S.K., Raushel F.M., Swaminathan S.
    Biochemistry 47:5608-5615(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) IN COMPLEX WITH INHIBITOR AND IRON IONS.

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 11, 2015
This is version 96 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.