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Protein

ATP phosphoribosyltransferase regulatory subunit

Gene

hisZ

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine (By similarity).By similarity

Pathwayi: L-histidine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.
Proteins known to be involved in the 9 steps of the subpathway in this organism are:
  1. ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (Tmari_1041), 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (Tmari_1043), Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (Tmari_1044)
  8. Probable histidinol-phosphatase (hisK)
  9. Histidinol dehydrogenase (Tmari_1045), Histidinol dehydrogenase (hisD)
This subpathway is part of the pathway L-histidine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, the pathway L-histidine biosynthesis and in Amino-acid biosynthesis.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Enzyme and pathway databases

BioCyciTMAR243274:GC6P-1072-MONOMER.
UniPathwayiUPA00031; UER00006.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP phosphoribosyltransferase regulatory subunit
Gene namesi
Name:hisZ
Ordered Locus Names:TM_1043
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 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 – 275275ATP phosphoribosyltransferase regulatory subunitPRO_0000171072Add
BLAST

Interactioni

Subunit structurei

Heteromultimer composed of HisG and HisZ subunits.By similarity

Protein-protein interaction databases

STRINGi243274.TM1043.

Structurei

Secondary structure

1
275
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1813Combined sources
Beta strandi28 – 314Combined sources
Beta strandi40 – 423Combined sources
Beta strandi47 – 504Combined sources
Helixi54 – 629Combined sources
Beta strandi65 – 673Combined sources
Beta strandi71 – 744Combined sources
Beta strandi77 – 837Combined sources
Beta strandi86 – 9914Combined sources
Helixi103 – 12018Combined sources
Beta strandi125 – 1317Combined sources
Helixi134 – 1396Combined sources
Beta strandi140 – 1423Combined sources
Helixi144 – 1463Combined sources
Helixi147 – 1559Combined sources
Helixi159 – 16810Combined sources
Helixi175 – 18511Combined sources
Helixi189 – 1935Combined sources
Helixi199 – 21517Combined sources
Beta strandi217 – 2237Combined sources
Helixi228 – 2325Combined sources
Beta strandi235 – 2439Combined sources
Turni244 – 2474Combined sources
Beta strandi248 – 25811Combined sources
Beta strandi261 – 27414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1USYX-ray2.52A/B/C/D1-275[»]
ProteinModelPortaliQ9X0D3.
SMRiQ9X0D3. Positions 1-275.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X0D3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0124. LUCA.
InParanoidiQ9X0D3.
KOiK01892.
OMAiIEDSIYR.
OrthoDBiEOG6F2956.

Family and domain databases

HAMAPiMF_00125. HisZ.
InterProiIPR004517. HisZ.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9X0D3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFLDFEKVF SFYSKATKKG FSPFFVPALE KAEEPAGNFF LDRKGNLFSI
60 70 80 90 100
REDFTKTVLN HRKRYSPDSQ IKVWYADFVY RYSGSDLVAE YQLGLEKVPR
110 120 130 140 150
NSLDDSLEVL EIIVESASEF FEGPVIVEIG HTGVYEDLLK EIPKDLHEKV
160 170 180 190 200
LNLIDTKNLA EIEFLSHMKK IDLSRVEKII EDSIYRRSPE HLKTMDLPLS
210 220 230 240 250
VREDLLSASS FLQEKFPTVS VEIDLTLART IEEYCGLIFT IYDTSSSRLV
260 270
AAGGEYTVNG EKGVGGSIFL EGKTC
Length:275
Mass (Da):31,289
Last modified:November 1, 1999 - v1
Checksum:iCFE7716DF9177EC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36120.1.
PIRiB72305.
RefSeqiNP_228849.1. NC_000853.1.
WP_010865251.1. NC_000853.1.

Genome annotation databases

EnsemblBacteriaiAAD36120; AAD36120; TM_1043.
GeneIDi897251.
KEGGitma:TM1043.
tmi:THEMA_09145.
PATRICi23937015. VBITheMar51294_1056.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36120.1.
PIRiB72305.
RefSeqiNP_228849.1. NC_000853.1.
WP_010865251.1. NC_000853.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1USYX-ray2.52A/B/C/D1-275[»]
ProteinModelPortaliQ9X0D3.
SMRiQ9X0D3. Positions 1-275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1043.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36120; AAD36120; TM_1043.
GeneIDi897251.
KEGGitma:TM1043.
tmi:THEMA_09145.
PATRICi23937015. VBITheMar51294_1056.

Phylogenomic databases

eggNOGiCOG0124. LUCA.
InParanoidiQ9X0D3.
KOiK01892.
OMAiIEDSIYR.
OrthoDBiEOG6F2956.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00006.
BioCyciTMAR243274:GC6P-1072-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9X0D3.

Family and domain databases

HAMAPiMF_00125. HisZ.
InterProiIPR004517. HisZ.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Entry informationi

Entry nameiHISZ_THEMA
AccessioniPrimary (citable) accession number: Q9X0D3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: November 1, 1999
Last modified: November 11, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This function is generally fulfilled by the C-terminal part of HisG, which is missing in some bacteria such as this one.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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

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.