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Protein

Histidine ammonia-lyase

Gene

hutH

Organism
Alkaliphilus metalliredigens (strain QYMF)
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:Amet_3149
OrganismiAlkaliphilus metalliredigens (strain QYMF)
Taxonomic identifieri293826 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus
Proteomesi
  • UP000001572 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_10001004311 – 507Histidine ammonia-lyaseAdd BLAST507

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki143 ↔ 1455-imidazolinone (Ser-Gly)By similarity
Modified residuei1442,3-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 Ser-Ser-Gly.UniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi293826.Amet_3149.

Structurei

3D structure databases

ProteinModelPortaliA6TSX0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PAL/histidase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C84. Bacteria.
COG2986. LUCA.
HOGENOMiHOG000237619.
KOiK01745.
OMAiLILSHAC.
OrthoDBiPOG091H04Z2.

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.

A6TSX0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVSINGND LTLEEMIMVA REYCSITIEP EAMVRVANTR KVVERYVEEE
60 70 80 90 100
RVVYGITTGF GKFSDVAISK DQTEMLQRNL IISHACGVGE PLKEEVVRGV
110 120 130 140 150
LLLRANALAK GYSGVRPNTL ETLINMLNKG VHPIIPEKGS LGSSGDLAPL
160 170 180 190 200
AHMVLVMMGE GEATYKGNKM SGKEAMEKAG IPPVVLSAKE GLALINGTQV
210 220 230 240 250
MTAIGALLIY DCQKLIKLAD IAGALTLEAQ RGIIDAFDHK VHRVRPHQGQ
260 270 280 290 300
QQTAQNIVNL VAGSTLITRQ GEVRVQDAYT LRCIPQIHGA SRDAIMYAVD
310 320 330 340 350
KVNIEINGAT DNPLIFPEED EVISGGNFHG QPMALTFDFL GIAIAELANV
360 370 380 390 400
SERRIERLVN PQLSGLPAFL TAKGGLNSGF MITQYAAASL VSENKILAHP
410 420 430 440 450
ASVDSIPSSA NQEDHVSMGT IAARKARSIY ENTVNVLGVE LMAASQAVEF
460 470 480 490 500
YDGYELGIGT RRAYDTIRKS VAHLDEDRVM YVDMNRCAEL VFNHKIVDEV

EKVVSIL
Length:507
Mass (Da):55,125
Last modified:August 21, 2007 - v1
Checksum:i669E6BB8F44CB3F0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000724 Genomic DNA. Translation: ABR49288.1.
RefSeqiWP_012064254.1. NC_009633.1.

Genome annotation databases

EnsemblBacteriaiABR49288; ABR49288; Amet_3149.
KEGGiamt:Amet_3149.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000724 Genomic DNA. Translation: ABR49288.1.
RefSeqiWP_012064254.1. NC_009633.1.

3D structure databases

ProteinModelPortaliA6TSX0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi293826.Amet_3149.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABR49288; ABR49288; Amet_3149.
KEGGiamt:Amet_3149.

Phylogenomic databases

eggNOGiENOG4105C84. Bacteria.
COG2986. LUCA.
HOGENOMiHOG000237619.
KOiK01745.
OMAiLILSHAC.
OrthoDBiPOG091H04Z2.

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_ALKMQ
AccessioniPrimary (citable) accession number: A6TSX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: August 21, 2007
Last modified: November 2, 2016
This is version 61 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, Reference 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.