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P21310

- HUTH_PSEPU

UniProt

P21310 - HUTH_PSEPU

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Protein
Histidine ammonia-lyase
Gene
hutH
Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-histidine = urocanate + NH3.4 Publications

Pathwayi

GO - Molecular functioni

  1. histidine ammonia-lyase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. biosynthetic process Source: InterPro
  2. histidine catabolic process to glutamate and formamide Source: UniProtKB-UniPathway
  3. histidine catabolic process to glutamate and formate Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Histidine metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11608.
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

Cytoplasm Reviewed prediction UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi113 – 1131S → A: No loss of activity.
Mutagenesisi144 – 1441S → A or T: Complete loss of activity. 3 Publications
Mutagenesisi144 – 1441S → C: No effect. 3 Publications
Mutagenesisi394 – 3941S → A: No loss of activity.
Mutagenesisi419 – 4191S → A: No loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 510509Histidine ammonia-lyaseUniRule annotation
PRO_0000161017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki143 ↔ 1455-imidazolinone (Ala-Gly)UniRule annotation
Modified residuei144 – 14412,3-didehydroalanine (Ser)UniRule annotation

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.UniRule annotation

Expressioni

Inductioni

By histidine and urocanate.UniRule annotation

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64
Helixi13 – 219
Beta strandi25 – 284
Helixi30 – 323
Helixi33 – 4816
Turni54 – 563
Helixi61 – 633
Helixi70 – 8415
Beta strandi88 – 914
Helixi94 – 10815
Turni109 – 1124
Helixi117 – 12913
Beta strandi131 – 1333
Beta strandi136 – 1383
Beta strandi142 – 1454
Helixi147 – 1559
Helixi156 – 1583
Beta strandi161 – 1655
Beta strandi168 – 1714
Helixi172 – 1787
Helixi190 – 1956
Beta strandi196 – 1983
Helixi199 – 22931
Helixi235 – 2373
Helixi239 – 2457
Helixi248 – 26114
Helixi266 – 2705
Turni271 – 2733
Helixi274 – 2763
Helixi281 – 2844
Helixi286 – 30823
Beta strandi314 – 3185
Turni319 – 3224
Beta strandi323 – 3253
Helixi333 – 36129
Helixi363 – 3664
Helixi370 – 3723
Turni376 – 3783
Helixi383 – 39917
Turni411 – 4144
Helixi421 – 45131
Helixi460 – 47011
Beta strandi478 – 4803
Helixi483 – 49412
Turni495 – 4984
Helixi499 – 5013
Beta strandi504 – 5074

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 2-510.

Miscellaneous databases

EvolutionaryTraceiP21310.

Family & Domainsi

Sequence similaritiesi

Belongs to the PAL/histidase family.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00229. His_ammonia_lyase.
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

MTELTLKPGT LTLAQLRAIH AAPVRLQLDA SAAPAIDASV ACVEQIIAED    50
RTAYGINTGF GLLASTRIAS HDLENLQRSL VLSHAAGIGA PLDDDLVRLI 100
MVLKINSLSR GFSGIRRKVI DALIALVNAE VYPHIPLKGS VGASGDLAPL 150
AHMSLVLLGE GKARYKGQWL SATEALAVAG LEPLTLAAKE GLALLNGTQA 200
STAYALRGLF YAEDLYAAAI ACGGLSVEAV LGSRSPFDAR IHEARGQRGQ 250
IDTAACFRDL LGDSSEVSLS HKNCDKVQDP YSLRCQPQVM GACLTQLRQA 300
AEVLGIEANA VSDNPLVFAA EGDVISGGNF HAEPVAMAAD NLALAIAEIG 350
SLSERRISLM MDKHMSQLPP FLVENGGVNS GFMIAQVTAA ALASENKALS 400
HPHSVDSLPT SANQEDHVSM APAAGKRLWE MAENTRGVLA IEWLGACQGL 450
DLRKGLKTSA KLEKARQALR SEVAHYDRDR FFAPDIEKAV ELLAKGSLTG 500
LLPAGVLPSL 510
Length:510
Mass (Da):53,761
Last modified:January 23, 2007 - v3
Checksum:i7D80C7E64B0C4F57
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521H → T in AAA25840. 1 Publication
Sequence conflicti439 – 4391L → P in AAA25840. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M35140 Genomic DNA. Translation: AAA25840.1.
PIRiA35251.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M35140 Genomic DNA. Translation: AAA25840.1 .
PIRi A35251.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B8F X-ray 2.10 A 2-510 [» ]
1EB4 X-ray 2.00 A 2-510 [» ]
1GK2 X-ray 1.90 A/B/C/D 2-510 [» ]
1GK3 X-ray 2.25 A 2-510 [» ]
1GKJ X-ray 1.70 A 2-510 [» ]
1GKM X-ray 1.00 A 2-510 [» ]
ProteinModelPortali P21310.
SMRi P21310. Positions 2-510.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00379 ; UER00549 .
BioCyci MetaCyc:MONOMER-11608.

Miscellaneous databases

EvolutionaryTracei P21310.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
HAMAPi MF_00229. His_ammonia_lyase.
InterProi IPR001106. Aromatic_Lyase.
IPR024083. Fumarase/histidase_N.
IPR005921. HutH.
IPR008948. L-Aspartase-like.
IPR022313. Phe/His_NH3-lyase_AS.
[Graphical view ]
Pfami PF00221. Lyase_aromatic. 1 hit.
[Graphical view ]
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR01225. hutH. 1 hit.
PROSITEi PS00488. PAL_HISTIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequence analysis of the hutH gene encoding histidine ammonia-lyase in Pseudomonas putida."
    Consevage M.W., Phillips A.T.
    J. Bacteriol. 172:2224-2229(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13.
    Strain: ATCC 12633 / DSM 291 / JCM 13063 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90.
  2. "Identification of Ser143 as the site of modification in the active site of histidine ammonia-lyase."
    Hernandez D., Stroh J.G., Phillips A.T.
    Arch. Biochem. Biophys. 307:126-132(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, INHIBITION BY CHEMICAL MODIFICATION, IDENTIFICATION BY MASS SPECTROMETRY.
  3. "Ser-143 is an essential active site residue in histidine ammonia-lyase of Pseudomonas putida."
    Hernandez D., Phillips A.T.
    Biochem. Biophys. Res. Commun. 201:1433-1438(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, INHIBITION BY CHEMICAL MODIFICATION, MUTAGENESIS OF SER-144.
  4. "Identification of serine-143 as the most likely precursor of dehydroalanine in the active site of histidine ammonia-lyase. A study of the overexpressed enzyme by site-directed mutagenesis."
    Langer M., Reck G., Reed J., Retey J.
    Biochemistry 33:6462-6467(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME MECHANISM, DEHYDROALANINE FORMATION, MUTAGENESIS OF SER-144.
  5. "Histidine ammonia-lyase mutant S143C is posttranslationally converted into fully active wild-type enzyme. Evidence for serine 143 to be the precursor of active site dehydroalanine."
    Langer M., Lieber A., Retey J.
    Biochemistry 33:14034-14038(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME MECHANISM, MUTAGENESIS OF SER-144.
  6. "Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile."
    Schwede T.F., Retey J., Schulz G.E.
    Biochemistry 38:5355-5361(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SEQUENCE REVISION TO 152 AND 439.
    Strain: ATCC 12633 / DSM 291 / JCM 13063 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90.

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: April 16, 2014
This is version 103 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

External Data

Dasty 3

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