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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
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

1-(5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide = 5-((5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide.

Pathway:iL-histidine biosynthesis

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:
  1. ATP phosphoribosyltransferase (Tmari_1046), 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 (hisA)
  5. Imidazole glycerol phosphate synthase amidotransferase subunit (Tmari_1042), Imidazole glycerol phosphate synthase cyclase subunit (Tmari_1040), 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)
  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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei8 – 81Proton acceptor1 Publication
Active sitei127 – 1271Proton donor1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00031; 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
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81D → N: Loss of activity. 1 Publication
Mutagenesisi48 – 481H → A: Decrease in activity. 1 Publication
Mutagenesisi51 – 511D → N: Decrease in activity. 1 Publication
Mutagenesisi83 – 831R → N: Decrease in activity. 1 Publication
Mutagenesisi127 – 1271D → N: Almost no activity. 1 Publication
Mutagenesisi164 – 1641T → A: Strong decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2412411-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerasePRO_0000142068Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi243274.TM1037.

Structurei

Secondary structure

1
241
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109Combined sources
Beta strandi13 – 175Combined sources
Helixi18 – 203Combined sources
Helixi22 – 243Combined sources
Beta strandi25 – 306Combined sources
Helixi32 – 4110Combined sources
Beta strandi47 – 515Combined sources
Helixi52 – 576Combined sources
Helixi63 – 686Combined sources
Helixi69 – 757Combined sources
Beta strandi76 – 816Combined sources
Helixi85 – 939Combined sources
Beta strandi98 – 1014Combined sources
Helixi103 – 1075Combined sources
Helixi111 – 1166Combined sources
Turni117 – 1193Combined sources
Beta strandi121 – 1299Combined sources
Helixi141 – 1444Combined sources
Helixi146 – 1549Combined sources
Turni155 – 1573Combined sources
Beta strandi160 – 1656Combined sources
Helixi168 – 1714Combined sources
Helixi177 – 18711Combined sources
Beta strandi190 – 1967Combined sources
Helixi200 – 21213Combined sources
Turni213 – 2153Combined sources
Beta strandi216 – 2227Combined sources
Helixi224 – 2274Combined sources
Helixi233 – 2408Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QO2X-ray1.85A/B1-241[»]
2CFFX-ray2.50A/B1-241[»]
2W79X-ray1.85A/B1-241[»]
ProteinModelPortaliQ9X0C7.
SMRiQ9X0C7. Positions 1-241.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X0C7.

Family & Domainsi

Sequence similaritiesi

Belongs to the HisA/HisF family.Curated

Phylogenomic databases

eggNOGiCOG0106.
InParanoidiQ9X0C7.
KOiK01814.
OMAiDGAKSKH.
OrthoDBiEOG6H1Q3W.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01014. HisA.
InterProiIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR006063. HisA.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR00007. TIGR00007. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9X0C7-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:241
Mass (Da):27,028
Last modified:November 1, 1999 - v1
Checksum:iB1ABDDE5A4D5213D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36114.1.
PIRiD72304.
RefSeqiNP_228843.1. NC_000853.1.
WP_004080485.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36114; AAD36114; TM_1037.
GeneIDi897150.
KEGGitma:TM1037.
tmi:THEMA_09175.
tmm:Tmari_1041.
PATRICi23937003. VBITheMar51294_1050.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36114.1.
PIRiD72304.
RefSeqiNP_228843.1. NC_000853.1.
WP_004080485.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QO2X-ray1.85A/B1-241[»]
2CFFX-ray2.50A/B1-241[»]
2W79X-ray1.85A/B1-241[»]
ProteinModelPortaliQ9X0C7.
SMRiQ9X0C7. Positions 1-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36114; AAD36114; TM_1037.
GeneIDi897150.
KEGGitma:TM1037.
tmi:THEMA_09175.
tmm:Tmari_1041.
PATRICi23937003. VBITheMar51294_1050.

Phylogenomic databases

eggNOGiCOG0106.
InParanoidiQ9X0C7.
KOiK01814.
OMAiDGAKSKH.
OrthoDBiEOG6H1Q3W.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00009.

Miscellaneous databases

EvolutionaryTraceiQ9X0C7.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01014. HisA.
InterProiIPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR006063. HisA.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00977. His_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR00007. TIGR00007. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. "Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis have similar reaction mechanisms and common strategies for protecting their labile substrates."
    Henn-Sax M., Thoma R., Schmidt S., Hennig M., Kirschner K., Sterner R.
    Biochemistry 41:12032-12042(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITES, SUBUNIT, MUTAGENESIS OF ASP-8; HIS-48; ASP-51; ARG-83; ASP-127 AND THR-164.
  3. "Structural evidence for evolution of the beta/alpha barrel scaffold by gene duplication and fusion."
    Lang D., Thoma R., Henn-Sax M., Sterner R., Wilmanns M.
    Science 289:1546-1550(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).

Entry informationi

Entry nameiHIS4_THEMA
AccessioniPrimary (citable) accession number: Q9X0C7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1999
Last modified: July 22, 2015
This is version 110 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

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

External Data

Dasty 3

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 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.