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Protein

Histidine ammonia-lyase

Gene

hutH

Organism
Staphylococcus aureus (strain MW2)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

L-histidine = urocanate + NH3.UniRule annotation

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.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Histidine ammonia-lyase (hutH)
  2. Urocanate hydratase (hutU)
  3. 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

UniPathwayiUPA00379; UER00549.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine ammonia-lyaseUniRule annotation (EC:4.3.1.3UniRule annotation)
Short name:
HistidaseUniRule annotation
Gene namesi
Name:hutHUniRule annotation
Ordered Locus Names:MW0008
OrganismiStaphylococcus aureus (strain MW2)
Taxonomic identifieri196620 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000418 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001610341 – 504Histidine ammonia-lyaseAdd BLAST504

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki142 ↔ 1445-imidazolinone (Ala-Gly)UniRule annotation
Modified residuei1432,3-didehydroalanine (Ser)UniRule annotation1

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

Structurei

3D structure databases

ProteinModelPortaliQ8NYY3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PAL/histidase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000237619.
KOiK01745.
OMAiLILSHAC.

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.

Q8NYY3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLYLDGETL TIEDIKSFLQ QQSKIEIIDD ALERVKKSRA VVERIIENEE
60 70 80 90 100
TVYGITTGFG LFSDVRIDPT QYNELQVNLI RSHACGLGEP FSKEVALVMM
110 120 130 140 150
ILRLNTLLKG HSGATLELVR QLQFFINERI IPIIPQQGSL GASGDLAPLS
160 170 180 190 200
HLALALIGEG KVLYRGEEKD SDDVLRELNR QPLNLQAKEG LALINGTQAM
210 220 230 240 250
TAQGVISYIE SEDLGYQSEW IAALTHQSLN GIIDAYRHDV HAVRNFQEQI
260 270 280 290 300
NVAARMRDWL EGSTLTTRQA EIRVQDAYTL RCIPQIHGAS FQVFNYVKQQ
310 320 330 340 350
LEFEMNAAND NPLIFEEANE TFVISGGNFH GQPIAFALDH LKLGVSELAN
360 370 380 390 400
VSERRLERLV NPQLNGDLPA FLSPEPGLQS GAMIMQYAAA SLVSENKTLA
410 420 430 440 450
HPASVDSITS SANQEDHVSM GTTAARHGYQ IIENARRVLA IECVIALQAA
460 470 480 490 500
ELKGVEGLSP KTRRKYEEFR SIVPSITHDR QFHKDIEAVA QYLKQSIYQT

TACH
Length:504
Mass (Da):56,090
Last modified:October 19, 2002 - v1
Checksum:i378A3419C5A122FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000033 Genomic DNA. Translation: BAB93873.1.
RefSeqiWP_000177468.1. NC_003923.1.

Genome annotation databases

EnsemblBacteriaiBAB93873; BAB93873; BAB93873.
KEGGisam:MW0008.
PATRICi19566448. VBIStaAur44266_0008.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000033 Genomic DNA. Translation: BAB93873.1.
RefSeqiWP_000177468.1. NC_003923.1.

3D structure databases

ProteinModelPortaliQ8NYY3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB93873; BAB93873; BAB93873.
KEGGisam:MW0008.
PATRICi19566448. VBIStaAur44266_0008.

Phylogenomic databases

HOGENOMiHOG000237619.
KOiK01745.
OMAiLILSHAC.

Enzyme and pathway databases

UniPathwayiUPA00379; UER00549.

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_STAAW
AccessioniPrimary (citable) accession number: Q8NYY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: November 2, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.