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Q9X0C7

- HIS4_THEMA

UniProt

Q9X0C7 - HIS4_THEMA

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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: 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.

Pathwayi

Sites

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

GO - Molecular functioni

  1. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. histidine biosynthetic process Source: UniProtKB-HAMAP
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: Chromosome

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
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.
OMAiKKENTIF.
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.
YP_007977390.1. NC_021214.1.
YP_008991867.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD36114; AAD36114; TM_1037.
GeneIDi18093681.
897150.
KEGGitma:TM1037.
PATRICi23937003. VBITheMar51294_1050.

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.
YP_007977390.1. NC_021214.1.
YP_008991867.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q9X0C7.
SMRi Q9X0C7. Positions 1-241.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243274.TM1037.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD36114 ; AAD36114 ; TM_1037 .
GeneIDi 18093681.
897150.
KEGGi tma:TM1037.
PATRICi 23937003. VBITheMar51294_1050.

Phylogenomic databases

eggNOGi COG0106.
InParanoidi Q9X0C7.
KOi K01814.
OMAi KKENTIF.
OrthoDBi EOG6H1Q3W.

Enzyme and pathway databases

UniPathwayi UPA00031 ; UER00009 .

Miscellaneous databases

EvolutionaryTracei Q9X0C7.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01014. HisA.
InterProi IPR013785. Aldolase_TIM.
IPR006062. His_biosynth.
IPR006063. HisA.
IPR023016. Isoase_HisA.
IPR011060. RibuloseP-bd_barrel.
[Graphical view ]
Pfami PF00977. His_biosynth. 1 hit.
[Graphical view ]
SUPFAMi SSF51366. SSF51366. 1 hit.
TIGRFAMsi TIGR00007. TIGR00007. 1 hit.
ProtoNeti Search...

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: November 26, 2014
This is version 104 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