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Protein

Urocanate hydratase

Gene

hutU

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H2O.

Cofactori

NAD+Note: Binds 1 NAD+ per subunit.

Pathwayi: L-histidine degradation into L-glutamate

This protein is involved in step 2 of the subpathway that synthesizes N-formimidoyl-L-glutamate from L-histidine.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Histidine ammonia-lyase (DW66_2585), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (PU99_10260), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (HA62_16700), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (HB13667_15065), Histidine ammonia-lyase (hutH_3), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH_1), Histidine ammonia-lyase (HB4184_14930), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (hutH), Histidine ammonia-lyase (AYO28_15945)
  2. Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU), Urocanate hydratase (hutU)
  3. Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), Imidazolonepropionase (hutI), 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
Active sitei4111

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Histidine metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11616.
BRENDAi4.2.1.49. 5092.
UniPathwayiUPA00379; UER00550.

Names & Taxonomyi

Protein namesi
Recommended name:
Urocanate hydratase (EC:4.2.1.49)
Short name:
Urocanase
Alternative name(s):
Imidazolonepropionate hydrolase
Gene namesi
Name:hutU
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi64C → A: No loss of activity. 1 Publication1
Mutagenesisi192C → A: No loss of activity. 1 Publication1
Mutagenesisi198C → A: No loss of activity. 1 Publication1
Mutagenesisi355C → A: Minor loss in activity. 1 Publication1
Mutagenesisi411C → A: Loss of activity. 1 Publication1
Mutagenesisi544C → A: No loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002073442 – 557Urocanate hydrataseAdd BLAST556

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi160488.PP_5033.

Structurei

Secondary structure

1557
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi21 – 24Combined sources4
Helixi25 – 37Combined sources13
Turni40 – 42Combined sources3
Helixi46 – 48Combined sources3
Beta strandi50 – 52Combined sources3
Turni53 – 55Combined sources3
Beta strandi56 – 61Combined sources6
Helixi62 – 74Combined sources13
Beta strandi79 – 84Combined sources6
Beta strandi87 – 93Combined sources7
Beta strandi100 – 106Combined sources7
Helixi110 – 112Combined sources3
Helixi115 – 123Combined sources9
Turni131 – 137Combined sources7
Helixi143 – 160Combined sources18
Beta strandi161 – 163Combined sources3
Beta strandi169 – 173Combined sources5
Turni177 – 180Combined sources4
Helixi181 – 188Combined sources8
Beta strandi192 – 198Combined sources7
Helixi200 – 208Combined sources9
Helixi219 – 231Combined sources13
Beta strandi237 – 242Combined sources6
Helixi244 – 254Combined sources11
Beta strandi259 – 261Combined sources3
Turni270 – 272Combined sources3
Helixi281 – 290Combined sources10
Helixi292 – 315Combined sources24
Helixi327 – 333Combined sources7
Helixi339 – 341Combined sources3
Helixi345 – 348Combined sources4
Helixi351 – 354Combined sources4
Turni355 – 357Combined sources3
Beta strandi361 – 365Combined sources5
Helixi370 – 383Combined sources14
Helixi388 – 400Combined sources13
Beta strandi408 – 410Combined sources3
Helixi417 – 430Combined sources14
Beta strandi433 – 436Combined sources4
Beta strandi438 – 442Combined sources5
Beta strandi449 – 451Combined sources3
Turni453 – 459Combined sources7
Helixi469 – 481Combined sources13
Beta strandi484 – 491Combined sources8
Turni492 – 494Combined sources3
Beta strandi500 – 508Combined sources9
Helixi512 – 535Combined sources24
Helixi539 – 547Combined sources9
Turni553 – 555Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UWKX-ray1.19A/B1-557[»]
1UWLX-ray1.76A/B1-557[»]
1W1UX-ray2.23A/B2-557[»]
2V7GX-ray2.00A/B/C/D2-557[»]
ProteinModelPortaliP25080.
SMRiP25080.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25080.

Family & Domainsi

Sequence similaritiesi

Belongs to the urocanase family.Curated

Phylogenomic databases

eggNOGiENOG4105CGP. Bacteria.
COG2987. LUCA.

Family and domain databases

HAMAPiMF_00577. HutU. 1 hit.
InterProiIPR023637. Urocanase.
IPR023636. Urocanase_CS.
[Graphical view]
PfamiPF01175. Urocanase. 1 hit.
[Graphical view]
PIRSFiPIRSF001423. Urocanate_hydrat. 1 hit.
SUPFAMiSSF111326. SSF111326. 1 hit.
TIGRFAMsiTIGR01228. hutU. 1 hit.
PROSITEiPS01233. UROCANASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25080-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDNNKYRDV EIRAPRGNKL TAKSWLTEAP LRMLMNNLDP QVAENPKELV
60 70 80 90 100
VYGGIGRAAR NWECYDKIVE TLTRLEDDET LLVQSGKPVG VFKTHSNAPR
110 120 130 140 150
VLIANSNLVP HWANWEHFNE LDAKGLAMYG QMTAGSWIYI GSQGIVQGTY
160 170 180 190 200
ETFVEAGRQH YGGTVKAKWV LTAGLGGMGG AQPLAATLAG ACSLNIECQQ
210 220 230 240 250
SRIDFRLETR YVDEQATDLD DALVRIAKYT AEGKAISIAL HGNAAEILPE
260 270 280 290 300
LVKRGVRPDM VTDQTSAHDP LNGYLPAGWT WEQYRDRAQT EPAAVVKAAK
310 320 330 340 350
QSMAVHVQAM LDFQKQGVPT FDYGNNIRQM AKEEGVANAF DFPGFVPAYI
360 370 380 390 400
RPLFCRGVGP FRWAALSGEA EDIYKTDAKV KELIPDDAHL HRWLDMARER
410 420 430 440 450
ISFQGLPARI CWVGLGLRAK LGLAFNEMVR SGELSAPVVI GRDHLDSGSV
460 470 480 490 500
SSPNRETEAM RDGSDAVSDW PLLNALLNTA GGATWVSLHH GGGVGMGFSQ
510 520 530 540 550
HSGMVIVCDG TDEAAERIAR VLTNDPGTGV MRHADAGYDI AIDCAKEQGL

DLPMITG
Length:557
Mass (Da):60,804
Last modified:January 23, 2007 - v2
Checksum:i5AFD1E3307F34434
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti164 – 167TVKA → SLKG in AAA50311 (Ref. 2) Curated4

Mass spectrometryi

Molecular mass is 60686±15 Da from positions 2 - 557. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58483 Genomic DNA. Translation: CAA41392.1.
M33923 Genomic DNA. Translation: AAA50311.1.
PIRiS17184. DWPSUP.
T45008.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X58483 Genomic DNA. Translation: CAA41392.1.
M33923 Genomic DNA. Translation: AAA50311.1.
PIRiS17184. DWPSUP.
T45008.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UWKX-ray1.19A/B1-557[»]
1UWLX-ray1.76A/B1-557[»]
1W1UX-ray2.23A/B2-557[»]
2V7GX-ray2.00A/B/C/D2-557[»]
ProteinModelPortaliP25080.
SMRiP25080.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi160488.PP_5033.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CGP. Bacteria.
COG2987. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00379; UER00550.
BioCyciMetaCyc:MONOMER-11616.
BRENDAi4.2.1.49. 5092.

Miscellaneous databases

EvolutionaryTraceiP25080.

Family and domain databases

HAMAPiMF_00577. HutU. 1 hit.
InterProiIPR023637. Urocanase.
IPR023636. Urocanase_CS.
[Graphical view]
PfamiPF01175. Urocanase. 1 hit.
[Graphical view]
PIRSFiPIRSF001423. Urocanate_hydrat. 1 hit.
SUPFAMiSSF111326. SSF111326. 1 hit.
TIGRFAMsiTIGR01228. hutU. 1 hit.
PROSITEiPS01233. UROCANASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHUTU_PSEPU
AccessioniPrimary (citable) accession number: P25080
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.