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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 Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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-lyasePRO_0000161017Add
BLAST

Amino acid modifications

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

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.

Structurei

Secondary structure

1
510
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Helixi13 – 219Combined sources
Beta strandi25 – 284Combined sources
Helixi30 – 323Combined sources
Helixi33 – 4816Combined sources
Turni54 – 563Combined sources
Helixi61 – 633Combined sources
Helixi70 – 8415Combined sources
Beta strandi88 – 914Combined sources
Helixi94 – 10815Combined sources
Turni109 – 1124Combined sources
Helixi117 – 12913Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi142 – 1454Combined sources
Helixi147 – 1559Combined sources
Helixi156 – 1583Combined sources
Beta strandi161 – 1655Combined sources
Beta strandi168 – 1714Combined sources
Helixi172 – 1787Combined sources
Helixi190 – 1956Combined sources
Beta strandi196 – 1983Combined sources
Helixi199 – 22931Combined sources
Helixi235 – 2373Combined sources
Helixi239 – 2457Combined sources
Helixi248 – 26114Combined sources
Helixi266 – 2705Combined sources
Turni271 – 2733Combined sources
Helixi274 – 2763Combined sources
Helixi281 – 2844Combined sources
Helixi286 – 30823Combined sources
Beta strandi314 – 3185Combined sources
Turni319 – 3224Combined sources
Beta strandi323 – 3253Combined sources
Helixi333 – 36129Combined sources
Helixi363 – 3664Combined sources
Helixi370 – 3723Combined sources
Turni376 – 3783Combined sources
Helixi383 – 39917Combined sources
Turni411 – 4144Combined sources
Helixi421 – 45131Combined sources
Helixi460 – 47011Combined sources
Beta strandi478 – 4803Combined sources
Helixi483 – 49412Combined sources
Turni495 – 4984Combined sources
Helixi499 – 5013Combined sources
Beta strandi504 – 5074Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21310.

Family & Domainsi

Sequence similaritiesi

Belongs to the PAL/histidase family.Curated

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

        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521H → T in AAA25840. (PubMed:2332400)Curated
Sequence conflicti439 – 4391L → P in AAA25840. (PubMed:2332400)Curated

Sequence databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35140 Genomic DNA. Translation: AAA25840.1 .
PIRi A35251.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 106 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