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Protein

Imidazolonepropionase

Gene

hutI

Organism
Streptococcus pyogenes serotype M49 (strain NZ131)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi81 – 811Zinc or ironUniRule annotation
Metal bindingi83 – 831Zinc or ironUniRule annotation
Binding sitei90 – 901SubstrateUniRule annotation
Binding sitei103 – 1031SubstrateUniRule annotation
Binding sitei153 – 1531SubstrateUniRule annotation
Binding sitei186 – 1861SubstrateUniRule annotation
Metal bindingi251 – 2511Zinc or ironUniRule annotation
Binding sitei254 – 2541SubstrateUniRule annotation
Metal bindingi326 – 3261Zinc or ironUniRule annotation

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:Spy49_1723c
OrganismiStreptococcus pyogenes serotype M49 (strain NZ131)
Taxonomic identifieri471876 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000001039 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 – 421421ImidazolonepropionasePRO_1000121560Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB5XIX5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HutI family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000218460.
KOiK01468.
OMAiDHCTHLT.

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.

B5XIX5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVADVLLTHF NQLFCLNDPG HPLTGQEMKK ATIVEDGYIA IKDGLIVALG
60 70 80 90 100
SGEPDAELVG PQTIMRSYKG KIATPGIIDC HTHLVYGGSR EHEFAKKLAG
110 120 130 140 150
VSYLDILAQG GGILSTVRAT RSASFDNLYQ KSKRLLDYML LHGVTTVEAK
160 170 180 190 200
SGYGLDWETE KRQLDVVAAL EKDHPIDLVS TFMAAHAIPE EYKGNPKAYL
210 220 230 240 250
DVIIKDMLPV VKEENLAEFC DIFCEKNVFT ADESRYLLSK AKEMGFKLRI
260 270 280 290 300
HADEIASIGG VDVAAELSAV SAEHLMMITD DGIAKLIGAG VIGNLLPATT
310 320 330 340 350
FSLMEDTYAP ARKMIDAGMA ITLSTDSNPG SCPTANMQFV MQLGCFMLRL
360 370 380 390 400
TPIEVLNAVT INAAYSVNRQ ERVGSLTVGK EADIAIFDAP NIDYPFYFFA
410 420
TNLIHQVYKK GQLTVDRGRI L
Length:421
Mass (Da):45,977
Last modified:November 25, 2008 - v1
Checksum:i968634DD31501D6C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000829 Genomic DNA. Translation: ACI61974.1.
RefSeqiWP_002982296.1. NC_011375.1.

Genome annotation databases

EnsemblBacteriaiACI61974; ACI61974; Spy49_1723c.
KEGGisoz:Spy49_1723c.
PATRICi19758592. VBIStrPyo129711_1782.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000829 Genomic DNA. Translation: ACI61974.1.
RefSeqiWP_002982296.1. NC_011375.1.

3D structure databases

ProteinModelPortaliB5XIX5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACI61974; ACI61974; Spy49_1723c.
KEGGisoz:Spy49_1723c.
PATRICi19758592. VBIStrPyo129711_1782.

Phylogenomic databases

HOGENOMiHOG000218460.
KOiK01468.
OMAiDHCTHLT.

Enzyme and pathway databases

UniPathwayiUPA00379; UER00551.

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_STRPZ
AccessioniPrimary (citable) accession number: B5XIX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 25, 2008
Last modified: September 7, 2016
This is version 52 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

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.