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Protein

Imidazolonepropionase

Gene

hutI

Organism
Bacillus subtilis (strain 168)
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 bindingi80 – 801Zinc or iron
Metal bindingi82 – 821Zinc or iron
Binding sitei89 – 891Substrate
Binding sitei102 – 1021Substrate
Binding sitei152 – 1521Substrate
Binding sitei185 – 1851Substrate
Metal bindingi249 – 2491Zinc or iron
Binding sitei252 – 2521Substrate
Metal bindingi324 – 3241Zinc 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

BioCyciBSUB:BSU39370-MONOMER.
MetaCyc:HUTIBACSU-MONOMER.
BRENDAi3.5.2.7. 658.
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:BSU39370
ORF Names:EE57B
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 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_0000160944Add
BLAST

Proteomic databases

PaxDbiP42084.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021246.

Structurei

Secondary structure

1
421
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 1512Combined sources
Helixi26 – 294Combined sources
Beta strandi35 – 439Combined sources
Beta strandi46 – 527Combined sources
Turni53 – 586Combined sources
Beta strandi60 – 667Combined sources
Beta strandi71 – 744Combined sources
Beta strandi76 – 783Combined sources
Helixi90 – 923Combined sources
Helixi93 – 975Combined sources
Helixi102 – 1076Combined sources
Helixi112 – 12110Combined sources
Helixi124 – 14017Combined sources
Beta strandi143 – 1497Combined sources
Helixi156 – 17217Combined sources
Beta strandi173 – 18614Combined sources
Helixi189 – 1913Combined sources
Helixi195 – 2039Combined sources
Helixi206 – 2116Combined sources
Beta strandi216 – 2227Combined sources
Helixi229 – 24113Combined sources
Beta strandi245 – 2506Combined sources
Beta strandi252 – 2543Combined sources
Helixi258 – 2647Combined sources
Beta strandi268 – 2725Combined sources
Helixi278 – 28710Combined sources
Beta strandi290 – 2934Combined sources
Helixi295 – 3006Combined sources
Helixi309 – 3146Combined sources
Beta strandi319 – 3213Combined sources
Turni327 – 3293Combined sources
Helixi335 – 34511Combined sources
Helixi350 – 3567Combined sources
Helixi359 – 3646Combined sources
Turni368 – 3703Combined sources
Beta strandi382 – 3898Combined sources
Helixi392 – 3954Combined sources
Beta strandi402 – 4076Combined sources
Beta strandi410 – 4145Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BB0X-ray2.00A/B1-421[»]
2G3FX-ray2.00A/B1-421[»]
ProteinModelPortaliP42084.
SMRiP42084. Positions 2-415.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42084.

Family & Domainsi

Sequence similaritiesi

Belongs to the HutI family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CI2. Bacteria.
COG1228. LUCA.
HOGENOMiHOG000218460.
InParanoidiP42084.
KOiK01468.
OMAiDHCTHLT.
PhylomeDBiP42084.

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.

P42084-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKQIDTILI NIGQLLTMES SGPRAGKSMQ DLHVIEDAVV GIHEQKIVFA
60 70 80 90 100
GQKGAEAGYE ADEIIDCSGR LVTPGLVDPH THLVFGGSRE KEMNLKLQGI
110 120 130 140 150
SYLDILAQGG GILSTVKDTR AASEEELLQK AHFHLQRMLS YGTTTAEVKS
160 170 180 190 200
GYGLEKETEL KQLRVAKKLH ESQPVDLVST FMGAHAIPPE YQNDPDDFLD
210 220 230 240 250
QMLSLLPEIK EQELASFADI FTETGVFTVS QSRRYLQKAA EAGFGLKIHA
260 270 280 290 300
DEIDPLGGAE LAGKLKAVSA DHLVGTSDEG IKKLAEAGTI AVLLPGTTFY
310 320 330 340 350
LGKSTYARAR AMIDEGVCVS LATDFNPGSS PTENIQLIMS IAALHLKMTA
360 370 380 390 400
EEIWHAVTVN AAYAIGKGEE AGQLKAGRSA DLVIWQAPNY MYIPYHYGVN
410 420
HVHQVMKNGT IVVNREGAIL G
Length:421
Mass (Da):45,564
Last modified:November 1, 1995 - v1
Checksum:iA0E1893961745771
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31856 Genomic DNA. Translation: BAA06642.1.
AL009126 Genomic DNA. Translation: CAB15973.1.
PIRiD69643.
RefSeqiNP_391816.1. NC_000964.3.
WP_003244327.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15973; CAB15973; BSU39370.
GeneIDi937531.
KEGGibsu:BSU39370.
PATRICi18979938. VBIBacSub10457_4131.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31856 Genomic DNA. Translation: BAA06642.1.
AL009126 Genomic DNA. Translation: CAB15973.1.
PIRiD69643.
RefSeqiNP_391816.1. NC_000964.3.
WP_003244327.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BB0X-ray2.00A/B1-421[»]
2G3FX-ray2.00A/B1-421[»]
ProteinModelPortaliP42084.
SMRiP42084. Positions 2-415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021246.

Protein family/group databases

MEROPSiM38.980.

Proteomic databases

PaxDbiP42084.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15973; CAB15973; BSU39370.
GeneIDi937531.
KEGGibsu:BSU39370.
PATRICi18979938. VBIBacSub10457_4131.

Phylogenomic databases

eggNOGiENOG4105CI2. Bacteria.
COG1228. LUCA.
HOGENOMiHOG000218460.
InParanoidiP42084.
KOiK01468.
OMAiDHCTHLT.
PhylomeDBiP42084.

Enzyme and pathway databases

UniPathwayiUPA00379; UER00551.
BioCyciBSUB:BSU39370-MONOMER.
MetaCyc:HUTIBACSU-MONOMER.
BRENDAi3.5.2.7. 658.

Miscellaneous databases

EvolutionaryTraceiP42084.

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_BACSU
AccessioniPrimary (citable) accession number: P42084
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 7, 2016
This is version 121 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.