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Protein

Histidine ammonia-lyase

Gene

hutH

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

Functioni

Catalytic activityi

L-histidine = urocanate + NH3.4 Publications

Pathwayi: L-histidine degradation into L-glutamate

This protein is involved in step 1 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 (hutH), Histidine ammonia-lyase (DW66_2585), 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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Histidine metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11608.
BRENDAi4.3.1.3. 5092.
UniPathwayiUPA00379; UER00549.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine ammonia-lyase (EC:4.3.1.3)
Short name:
Histidase
Gene namesi
Name:hutH
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
Mutagenesisi113S → A: No loss of activity. 1
Mutagenesisi144S → A or T: Complete loss of activity. 3 Publications1
Mutagenesisi144S → C: No effect. 3 Publications1
Mutagenesisi394S → A: No loss of activity. 1
Mutagenesisi419S → A: No loss of activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001610172 – 510Histidine ammonia-lyaseAdd BLAST509

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki143 ↔ 1455-imidazolinone (Ala-Gly)
Modified residuei1442,3-didehydroalanine (Ser)1

Post-translational modificationi

Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.

Expressioni

Inductioni

By histidine and urocanate.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi160488.PP_5032.

Structurei

Secondary structure

1510
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Helixi13 – 21Combined sources9
Beta strandi25 – 28Combined sources4
Helixi30 – 32Combined sources3
Helixi33 – 48Combined sources16
Turni54 – 56Combined sources3
Helixi61 – 63Combined sources3
Helixi70 – 84Combined sources15
Beta strandi88 – 91Combined sources4
Helixi94 – 108Combined sources15
Turni109 – 112Combined sources4
Helixi117 – 129Combined sources13
Beta strandi131 – 133Combined sources3
Beta strandi136 – 138Combined sources3
Beta strandi142 – 145Combined sources4
Helixi147 – 155Combined sources9
Helixi156 – 158Combined sources3
Beta strandi161 – 165Combined sources5
Beta strandi168 – 171Combined sources4
Helixi172 – 178Combined sources7
Helixi190 – 195Combined sources6
Beta strandi196 – 198Combined sources3
Helixi199 – 229Combined sources31
Helixi235 – 237Combined sources3
Helixi239 – 245Combined sources7
Helixi248 – 261Combined sources14
Helixi266 – 270Combined sources5
Turni271 – 273Combined sources3
Helixi274 – 276Combined sources3
Helixi281 – 284Combined sources4
Helixi286 – 308Combined sources23
Beta strandi314 – 318Combined sources5
Turni319 – 322Combined sources4
Beta strandi323 – 325Combined sources3
Helixi333 – 361Combined sources29
Helixi363 – 366Combined sources4
Helixi370 – 372Combined sources3
Turni376 – 378Combined sources3
Helixi383 – 399Combined sources17
Turni411 – 414Combined sources4
Helixi421 – 451Combined sources31
Helixi460 – 470Combined sources11
Beta strandi478 – 480Combined sources3
Helixi483 – 494Combined sources12
Turni495 – 498Combined sources4
Helixi499 – 501Combined sources3
Beta strandi504 – 507Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B8FX-ray2.10A2-510[»]
1EB4X-ray2.00A2-510[»]
1GK2X-ray1.90A/B/C/D2-510[»]
1GK3X-ray2.25A2-510[»]
1GKJX-ray1.70A2-510[»]
1GKMX-ray1.00A2-510[»]
ProteinModelPortaliP21310.
SMRiP21310.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21310.

Family & Domainsi

Sequence similaritiesi

Belongs to the PAL/histidase family.Curated

Phylogenomic databases

eggNOGiENOG4105C84. Bacteria.
COG2986. LUCA.
KOiK01745.

Family and domain databases

CDDicd00332. PAL-HAL. 1 hit.
Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00229. His_ammonia_lyase. 1 hit.
InterProiIPR001106. Aromatic_Lyase.
IPR024083. Fumarase/histidase_N.
IPR005921. HutH.
IPR008948. L-Aspartase-like.
IPR022313. Phe/His_NH3-lyase_AS.
[Graphical view]
PfamiPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR01225. hutH. 1 hit.
PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P21310-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTELTLKPGT LTLAQLRAIH AAPVRLQLDA SAAPAIDASV ACVEQIIAED
60 70 80 90 100
RTAYGINTGF GLLASTRIAS HDLENLQRSL VLSHAAGIGA PLDDDLVRLI
110 120 130 140 150
MVLKINSLSR GFSGIRRKVI DALIALVNAE VYPHIPLKGS VGASGDLAPL
160 170 180 190 200
AHMSLVLLGE GKARYKGQWL SATEALAVAG LEPLTLAAKE GLALLNGTQA
210 220 230 240 250
STAYALRGLF YAEDLYAAAI ACGGLSVEAV LGSRSPFDAR IHEARGQRGQ
260 270 280 290 300
IDTAACFRDL LGDSSEVSLS HKNCDKVQDP YSLRCQPQVM GACLTQLRQA
310 320 330 340 350
AEVLGIEANA VSDNPLVFAA EGDVISGGNF HAEPVAMAAD NLALAIAEIG
360 370 380 390 400
SLSERRISLM MDKHMSQLPP FLVENGGVNS GFMIAQVTAA ALASENKALS
410 420 430 440 450
HPHSVDSLPT SANQEDHVSM APAAGKRLWE MAENTRGVLA IEWLGACQGL
460 470 480 490 500
DLRKGLKTSA KLEKARQALR SEVAHYDRDR FFAPDIEKAV ELLAKGSLTG
510
LLPAGVLPSL
Length:510
Mass (Da):53,761
Last modified:January 23, 2007 - v3
Checksum:i7D80C7E64B0C4F57
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti152H → T in AAA25840 (PubMed:2332400).Curated1
Sequence conflicti439L → P in AAA25840 (PubMed:2332400).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35140 Genomic DNA. Translation: AAA25840.1.
PIRiA35251.
RefSeqiWP_016502005.1. NZ_LWDW01000012.1.

Genome annotation databases

KEGGiag:AAA25840.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35140 Genomic DNA. Translation: AAA25840.1.
PIRiA35251.
RefSeqiWP_016502005.1. NZ_LWDW01000012.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B8FX-ray2.10A2-510[»]
1EB4X-ray2.00A2-510[»]
1GK2X-ray1.90A/B/C/D2-510[»]
1GK3X-ray2.25A2-510[»]
1GKJX-ray1.70A2-510[»]
1GKMX-ray1.00A2-510[»]
ProteinModelPortaliP21310.
SMRiP21310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi160488.PP_5032.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA25840.

Phylogenomic databases

eggNOGiENOG4105C84. Bacteria.
COG2986. LUCA.
KOiK01745.

Enzyme and pathway databases

UniPathwayiUPA00379; UER00549.
BioCyciMetaCyc:MONOMER-11608.
BRENDAi4.3.1.3. 5092.

Miscellaneous databases

EvolutionaryTraceiP21310.

Family and domain databases

CDDicd00332. PAL-HAL. 1 hit.
Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00229. His_ammonia_lyase. 1 hit.
InterProiIPR001106. Aromatic_Lyase.
IPR024083. Fumarase/histidase_N.
IPR005921. HutH.
IPR008948. L-Aspartase-like.
IPR022313. Phe/His_NH3-lyase_AS.
[Graphical view]
PfamiPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR01225. hutH. 1 hit.
PROSITEiPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHUTH_PSEPU
AccessioniPrimary (citable) accession number: P21310
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 119 of the entry and version 3 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.