UniProtKB - P42084 (HUTI_BACSU)
Protein
Imidazolonepropionase
Gene
hutI
Organism
Bacillus subtilis (strain 168)
Status
Functioni
Catalytic activityi
- EC:3.5.2.7UniRule annotation
Cofactori
: L-histidine degradation into L-glutamate Pathwayi
This protein is involved in step 3 of the subpathway that synthesizes N-formimidoyl-L-glutamate from L-histidine.UniRule annotationProteins known to be involved in the 3 steps of the subpathway in this organism are:
- Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH)
- Urocanate hydratase (hutU), Urocanate hydratase (hutU)
- Imidazolonepropionase (hutI), Imidazolonepropionase (hutI)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 80 | Zinc or iron | 1 | |
Metal bindingi | 82 | Zinc or iron | 1 | |
Binding sitei | 89 | Substrate | 1 | |
Binding sitei | 102 | Substrate | 1 | |
Binding sitei | 152 | Substrate | 1 | |
Binding sitei | 185 | Substrate | 1 | |
Metal bindingi | 249 | Zinc or iron | 1 | |
Binding sitei | 252 | Substrate | 1 | |
Metal bindingi | 324 | Zinc or iron | 1 |
GO - Molecular functioni
- imidazolonepropionase activity Source: GO_Central
- iron ion binding Source: UniProtKB-UniRule
- zinc ion binding Source: UniProtKB-UniRule
GO - Biological processi
- histidine catabolic process Source: GO_Central
- histidine catabolic process to glutamate and formamide Source: UniProtKB-UniPathway
- histidine catabolic process to glutamate and formate Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Hydrolase |
Biological process | Histidine metabolism |
Ligand | Iron, Metal-binding, Zinc |
Enzyme and pathway databases
BioCyci | BSUB:BSU39370-MONOMER MetaCyc:HUTIBACSU-MONOMER |
BRENDAi | 3.5.2.7, 658 |
UniPathwayi | UPA00379;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:BSU39370 ORF Names:EE57B |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000160944 | 1 – 421 | ImidazolonepropionaseAdd BLAST | 421 |
Proteomic databases
PaxDbi | P42084 |
Interactioni
Subunit structurei
Homodimer.
1 PublicationProtein-protein interaction databases
STRINGi | 224308.BSU39370 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P42084 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P42084 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG1228, Bacteria |
InParanoidi | P42084 |
OMAi | CNPGSSF |
PhylomeDBi | P42084 |
Family and domain databases
CDDi | cd01296, Imidazolone-5PH, 1 hit |
Gene3Di | 2.30.40.10, 1 hit |
HAMAPi | MF_00372, HutI, 1 hit |
InterProi | View protein in InterPro IPR006680, Amidohydro-rel IPR005920, HutI IPR011059, Metal-dep_hydrolase_composite IPR032466, Metal_Hydrolase |
PANTHERi | PTHR42752, PTHR42752, 1 hit |
Pfami | View protein in Pfam PF01979, Amidohydro_1, 1 hit |
SUPFAMi | SSF51338, SSF51338, 2 hits SSF51556, SSF51556, 1 hit |
TIGRFAMsi | TIGR01224, hutI, 1 hit |
i Sequence
Sequence statusi: Complete.
P42084-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D31856 Genomic DNA Translation: BAA06642.1 AL009126 Genomic DNA Translation: CAB15973.1 |
PIRi | D69643 |
RefSeqi | NP_391816.1, NC_000964.3 WP_003244327.1, NZ_JNCM01000034.1 |
Genome annotation databases
EnsemblBacteriai | CAB15973; CAB15973; BSU_39370 |
GeneIDi | 937531 |
KEGGi | bsu:BSU39370 |
PATRICi | fig|224308.179.peg.4262 |
Similar proteinsi
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 |
PIRi | D69643 |
RefSeqi | NP_391816.1, NC_000964.3 WP_003244327.1, NZ_JNCM01000034.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2BB0 | X-ray | 2.00 | A/B | 1-421 | [»] | |
2G3F | X-ray | 2.00 | A/B | 1-421 | [»] | |
SMRi | P42084 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU39370 |
Proteomic databases
PaxDbi | P42084 |
Genome annotation databases
EnsemblBacteriai | CAB15973; CAB15973; BSU_39370 |
GeneIDi | 937531 |
KEGGi | bsu:BSU39370 |
PATRICi | fig|224308.179.peg.4262 |
Phylogenomic databases
eggNOGi | COG1228, Bacteria |
InParanoidi | P42084 |
OMAi | CNPGSSF |
PhylomeDBi | P42084 |
Enzyme and pathway databases
UniPathwayi | UPA00379;UER00551 |
BioCyci | BSUB:BSU39370-MONOMER MetaCyc:HUTIBACSU-MONOMER |
BRENDAi | 3.5.2.7, 658 |
Miscellaneous databases
EvolutionaryTracei | P42084 |
Family and domain databases
CDDi | cd01296, Imidazolone-5PH, 1 hit |
Gene3Di | 2.30.40.10, 1 hit |
HAMAPi | MF_00372, HutI, 1 hit |
InterProi | View protein in InterPro IPR006680, Amidohydro-rel IPR005920, HutI IPR011059, Metal-dep_hydrolase_composite IPR032466, Metal_Hydrolase |
PANTHERi | PTHR42752, PTHR42752, 1 hit |
Pfami | View protein in Pfam PF01979, Amidohydro_1, 1 hit |
SUPFAMi | SSF51338, SSF51338, 2 hits SSF51556, SSF51556, 1 hit |
TIGRFAMsi | TIGR01224, hutI, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HUTI_BACSU | |
Accessioni | P42084Primary (citable) accession number: P42084 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | November 1, 1995 | |
Last modified: | April 7, 2021 | |
This is version 145 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families