UniProtKB - Q9X0C7 (HIS4_THEMA)
Protein
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase
Gene
hisA
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Functioni
Catalytic activityi
- 1-(5-phospho-β-D-ribosyl)-5-[(5-phospho-β-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamideEC:5.3.1.16
: L-histidine biosynthesis Pathwayi
This protein is involved in step 4 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:
- ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase regulatory subunit (hisZ)
- Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI)
- Histidine biosynthesis bifunctional protein HisIE (hisI), Histidine biosynthesis bifunctional protein HisIE (hisI)
- 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA), 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
- Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisF (hisF)
- Imidazoleglycerol-phosphate dehydratase (hisB), Imidazoleglycerol-phosphate dehydratase (hisB)
- Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC)
- Histidinol-phosphatase (Tmari_0805), Probable histidinol-phosphatase (hisK)
- Histidinol dehydrogenase (hisD), Histidinol dehydrogenase (hisD)
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.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 8 | Proton acceptor1 Publication | 1 | |
Active sitei | 127 | Proton donor1 Publication | 1 |
GO - Molecular functioni
- 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity Source: GO_Central
GO - Biological processi
- histidine biosynthetic process Source: GO_Central
- tryptophan biosynthetic process Source: GO_Central
Keywordsi
Molecular function | Isomerase |
Biological process | Amino-acid biosynthesis, Histidine biosynthesis |
Enzyme and pathway databases
UniPathwayi | UPA00031;UER00009 |
Names & Taxonomyi
Protein namesi | Recommended name: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (EC:5.3.1.16)Alternative name(s): Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase |
Gene namesi | Name:hisA Ordered Locus Names:TM_1037 |
Organismi | Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) |
Taxonomic identifieri | 243274 [NCBI] |
Taxonomic lineagei | Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › |
Proteomesi |
|
Subcellular locationi
- Cytoplasm By similarity
GO - Cellular componenti
- cytoplasm Source: GO_Central
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 8 | D → N: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 48 | H → A: Decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 51 | D → N: Decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 83 | R → N: Decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 127 | D → N: Almost no activity. 1 Publication | 1 | |
Mutagenesisi | 164 | T → A: Strong decrease in activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000142068 | 1 – 241 | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomeraseAdd BLAST | 241 |
Proteomic databases
PRIDEi | Q9X0C7 |
Interactioni
Subunit structurei
Monomer.
1 PublicationProtein-protein interaction databases
STRINGi | 243274.THEMA_09175 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q9X0C7 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9X0C7 |
Family & Domainsi
Sequence similaritiesi
Belongs to the HisA/HisF family.Curated
Phylogenomic databases
eggNOGi | COG0106, Bacteria |
InParanoidi | Q9X0C7 |
OMAi | EWLHLVD |
OrthoDBi | 794219at2 |
Family and domain databases
CDDi | cd04732, HisA, 1 hit |
Gene3Di | 3.20.20.70, 1 hit |
HAMAPi | MF_01014, HisA, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR006062, His_biosynth IPR006063, HisA IPR023016, Isoase_HisA-like IPR011060, RibuloseP-bd_barrel |
Pfami | View protein in Pfam PF00977, His_biosynth, 1 hit |
SUPFAMi | SSF51366, SSF51366, 1 hit |
TIGRFAMsi | TIGR00007, TIGR00007, 1 hit |
i Sequence
Sequence statusi: Complete.
Q9X0C7-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLVVPAIDLF RGKVARMIKG RKENTIFYEK DPVELVEKLI EEGFTLIHVV
60 70 80 90 100
DLSNAIENSG ENLPVLEKLS EFAEHIQIGG GIRSLDYAEK LRKLGYRRQI
110 120 130 140 150
VSSKVLEDPS FLKSLREIDV EPVFSLDTRG GRVAFKGWLA EEEIDPVSLL
160 170 180 190 200
KRLKEYGLEE IVHTEIEKDG TLQEHDFSLT KKIAIEAEVK VLAAGGISSE
210 220 230 240
NSLKTAQKVH TETNGLLKGV IVGRAFLEGI LTVEVMKRYA R
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE000512 Genomic DNA Translation: AAD36114.1 |
PIRi | D72304 |
RefSeqi | NP_228843.1, NC_000853.1 WP_004080485.1, NZ_CP011107.1 |
Genome annotation databases
EnsemblBacteriai | AAD36114; AAD36114; TM_1037 |
KEGGi | tma:TM1037 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE000512 Genomic DNA Translation: AAD36114.1 |
PIRi | D72304 |
RefSeqi | NP_228843.1, NC_000853.1 WP_004080485.1, NZ_CP011107.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1QO2 | X-ray | 1.85 | A/B | 1-241 | [»] | |
2CFF | X-ray | 2.50 | A/B | 1-241 | [»] | |
2W79 | X-ray | 1.85 | A/B | 1-241 | [»] | |
SMRi | Q9X0C7 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 243274.THEMA_09175 |
Proteomic databases
PRIDEi | Q9X0C7 |
Genome annotation databases
EnsemblBacteriai | AAD36114; AAD36114; TM_1037 |
KEGGi | tma:TM1037 |
Phylogenomic databases
eggNOGi | COG0106, Bacteria |
InParanoidi | Q9X0C7 |
OMAi | EWLHLVD |
OrthoDBi | 794219at2 |
Enzyme and pathway databases
UniPathwayi | UPA00031;UER00009 |
Miscellaneous databases
EvolutionaryTracei | Q9X0C7 |
Family and domain databases
CDDi | cd04732, HisA, 1 hit |
Gene3Di | 3.20.20.70, 1 hit |
HAMAPi | MF_01014, HisA, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR006062, His_biosynth IPR006063, HisA IPR023016, Isoase_HisA-like IPR011060, RibuloseP-bd_barrel |
Pfami | View protein in Pfam PF00977, His_biosynth, 1 hit |
SUPFAMi | SSF51366, SSF51366, 1 hit |
TIGRFAMsi | TIGR00007, TIGR00007, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HIS4_THEMA | |
Accessioni | Q9X0C7Primary (citable) accession number: Q9X0C7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 2, 2002 |
Last sequence update: | November 1, 1999 | |
Last modified: | December 2, 2020 | |
This is version 134 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families