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Protein

Imidazolonepropionase

Gene

hutI

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 bindingi73Zinc or ironUniRule annotation1
Metal bindingi75Zinc or ironUniRule annotation1
Binding sitei82SubstrateUniRule annotation1
Binding sitei95SubstrateUniRule annotation1
Binding sitei145SubstrateUniRule annotation1
Binding sitei178SubstrateUniRule annotation1
Metal bindingi243Zinc or ironUniRule annotation1
Binding sitei246SubstrateUniRule annotation1
Metal bindingi318Zinc or ironUniRule annotation1

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.

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:bll6243
OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Taxonomic identifieri224911 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
Proteomesi
  • UP000002526 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_00003064401 – 404ImidazolonepropionaseAdd BLAST404

Interactioni

Protein-protein interaction databases

STRINGi224911.bll6243.

Structurei

3D structure databases

ProteinModelPortaliQ89GV2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HutI family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CI2. Bacteria.
COG1228. LUCA.
HOGENOMiHOG000218461.
InParanoidiQ89GV2.
KOiK01468.
OMAiDHCTHLT.
OrthoDBiPOG091H0EIK.
PhylomeDBiQ89GV2.

Family and domain databases

CDDicd01296. Imidazolone-5PH. 1 hit.
Gene3Di2.30.40.10. 2 hits.
HAMAPiMF_00372. HutI. 1 hit.
InterProiIPR013108. Amidohydro_3.
IPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF07969. Amidohydro_3. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR01224. hutI. 1 hit.

Sequencei

Sequence statusi: Complete.

Q89GV2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAERFDRIWH NARLATMRAD RPDLGEIEHG LIAARGGHIV YAGAAADFPA
60 70 80 90 100
DADAIKRIDC AGRWITPGLV DCHTHLVYGG NRAHEFELRL KGASYEEIAR
110 120 130 140 150
AGGGIVSTVA ATRKASEAEL VASALPRLDA LIGEGATTVE IKSGYGLDAE
160 170 180 190 200
TEMRQLAAAR SLGRQRPVAI RTSFLGAHAL PPEADGDKDR YIDLVCKEML
210 220 230 240 250
PAVAKAGLAD AVDTFMEGIA FSAGQTARVF ETARGLGLPV KLHADQLSNL
260 270 280 290 300
GGAALAAKFS ALSADHLEHT DEAGAAAMAK AGTVAVLLPG AFYFIRETQK
310 320 330 340 350
PPVESFRKHG VHMALASDCN PGSSPLTSLL LAMNMGATLF RMTVAECLAG
360 370 380 390 400
VTREGAHALG VLDETGTLEA GKWCDLAIWD IERPAELVYR IGFNPLHRRV

WRGQ
Length:404
Mass (Da):43,021
Last modified:June 1, 2003 - v1
Checksum:iBC62ED8A047121EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000040 Genomic DNA. Translation: BAC51508.1.
RefSeqiNP_772883.1. NC_004463.1.
WP_011088983.1. NZ_CP011360.1.

Genome annotation databases

EnsemblBacteriaiBAC51508; BAC51508; BAC51508.
GeneIDi1054564.
KEGGibja:bll6243.
PATRICi21196294. VBIBraJap65052_6382.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000040 Genomic DNA. Translation: BAC51508.1.
RefSeqiNP_772883.1. NC_004463.1.
WP_011088983.1. NZ_CP011360.1.

3D structure databases

ProteinModelPortaliQ89GV2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224911.bll6243.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC51508; BAC51508; BAC51508.
GeneIDi1054564.
KEGGibja:bll6243.
PATRICi21196294. VBIBraJap65052_6382.

Phylogenomic databases

eggNOGiENOG4105CI2. Bacteria.
COG1228. LUCA.
HOGENOMiHOG000218461.
InParanoidiQ89GV2.
KOiK01468.
OMAiDHCTHLT.
OrthoDBiPOG091H0EIK.
PhylomeDBiQ89GV2.

Enzyme and pathway databases

UniPathwayiUPA00379; UER00551.

Family and domain databases

CDDicd01296. Imidazolone-5PH. 1 hit.
Gene3Di2.30.40.10. 2 hits.
HAMAPiMF_00372. HutI. 1 hit.
InterProiIPR013108. Amidohydro_3.
IPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF07969. Amidohydro_3. 1 hit.
[Graphical view]
SUPFAMiSSF51338. SSF51338. 2 hits.
SSF51556. SSF51556. 1 hit.
TIGRFAMsiTIGR01224. hutI. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHUTI_BRADU
AccessioniPrimary (citable) accession number: Q89GV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 81 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.