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Protein

Histidine ammonia-lyase

Gene

hutH

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

L-histidine = urocanate + NH3.

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)
  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

BioCyciBSUB:BSU39350-MONOMER.
MetaCyc:MONOMER-11609.
UniPathwayiUPA00379; UER00549.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidine ammonia-lyase (EC:4.3.1.3)
Short name:
Histidase
Gene namesi
Name:hutH
Ordered Locus Names:BSU39350
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508Histidine ammonia-lyasePRO_0000160991Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki141 ↔ 1435-imidazolinone (Ala-Gly)By similarity
Modified residuei142 – 14212,3-didehydroalanine (Ser)By similarity

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.By similarity

Proteomic databases

PaxDbiP10944.

Expressioni

Inductioni

By histidine.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021236.

Structurei

3D structure databases

ProteinModelPortaliP10944.
SMRiP10944. Positions 2-501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PAL/histidase family.Curated

Phylogenomic databases

eggNOGiENOG4105C84. Bacteria.
COG2986. LUCA.
HOGENOMiHOG000237619.
InParanoidiP10944.
KOiK01745.
OMAiLILSHAC.
PhylomeDBiP10944.

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.

P10944-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTLDGSSLT TADVARVLFD FEEAAASEES MERVKKSRAA VERIVRDEKT
60 70 80 90 100
IYGINTGFGK FSDVLIQKED SAALQLNLIL SHACGVGDPF PECVSRAMLL
110 120 130 140 150
LRANALLKGF SGVRAELIEQ LLAFLNKRVH PVIPQQGSLG ASGDLAPLSH
160 170 180 190 200
LALALIGQGE VFFEGERMPA MTGLKKAGIQ PVTLTSKEGL ALINGTQAMT
210 220 230 240 250
AMGVVAYIEA EKLAYQTERI ASLTIEGLQG IIDAFDEDIH LARGYQEQID
260 270 280 290 300
VAERIRFYLS DSGLTTSQGE LRVQDAYSLR CIPQVHGATW QTLGYVKEKL
310 320 330 340 350
EIEMNAATDN PLIFNDGDKV ISGGNFHGQP IAFAMDFLKI AISELANIAE
360 370 380 390 400
RRIERLVNPQ LNDLPPFLSP HPGLQSGAMI MQYAAASLVS ENKTLAHPAS
410 420 430 440 450
VDSIPSSANQ EDHVSMGTIA ARHAYQVIAN TRRVIAIEAI CALQAVEYRG
460 470 480 490 500
IEHAASYTKQ LFQEMRKVVP SIQQDRVFSY DIERLTDWLK KESLIPDHQN

KELRGMNI
Length:508
Mass (Da):55,675
Last modified:July 1, 1989 - v1
Checksum:i869C323BFCC318E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20659 Genomic DNA. Translation: AAA22538.1.
D31856 Genomic DNA. Translation: BAA06644.1.
AL009126 Genomic DNA. Translation: CAB15971.1.
PIRiS18810. UFBSHS.
RefSeqiNP_391814.1. NC_000964.3.
WP_003243255.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15971; CAB15971; BSU39350.
GeneIDi937541.
KEGGibsu:BSU39350.
PATRICi18979934. VBIBacSub10457_4129.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20659 Genomic DNA. Translation: AAA22538.1.
D31856 Genomic DNA. Translation: BAA06644.1.
AL009126 Genomic DNA. Translation: CAB15971.1.
PIRiS18810. UFBSHS.
RefSeqiNP_391814.1. NC_000964.3.
WP_003243255.1. NZ_JNCM01000034.1.

3D structure databases

ProteinModelPortaliP10944.
SMRiP10944. Positions 2-501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021236.

Proteomic databases

PaxDbiP10944.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15971; CAB15971; BSU39350.
GeneIDi937541.
KEGGibsu:BSU39350.
PATRICi18979934. VBIBacSub10457_4129.

Phylogenomic databases

eggNOGiENOG4105C84. Bacteria.
COG2986. LUCA.
HOGENOMiHOG000237619.
InParanoidiP10944.
KOiK01745.
OMAiLILSHAC.
PhylomeDBiP10944.

Enzyme and pathway databases

UniPathwayiUPA00379; UER00549.
BioCyciBSUB:BSU39350-MONOMER.
MetaCyc:MONOMER-11609.

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_BACSU
AccessioniPrimary (citable) accession number: P10944
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 7, 2016
This is version 124 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.