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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Pathwayi: L-histidine biosynthesis

This protein is involved in step 7 of the subpathway that synthesizes L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation
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 (hisA), 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 (hisB), Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC)
  8. Probable histidinol-phosphatase (hisK)
  9. Histidinol dehydrogenase (hisD), 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 - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Histidine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.6.1.9. 6331.
SABIO-RKQ9X0D0.
UniPathwayiUPA00031; UER00012.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol-phosphate aminotransferaseUniRule annotation (EC:2.6.1.9UniRule annotation)
Alternative name(s):
Imidazole acetol-phosphate transaminaseUniRule annotation
Gene namesi
Name:hisCUniRule annotation
Ordered Locus Names:TM_1040
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 335335Histidinol-phosphate aminotransferasePRO_0000153470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-(pyridoxal phosphate)lysine

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi243274.TM1040.

Structurei

Secondary structure

1
335
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 54Combined sources
Beta strandi21 – 266Combined sources
Helixi35 – 439Combined sources
Helixi47 – 515Combined sources
Helixi59 – 6911Combined sources
Helixi76 – 783Combined sources
Beta strandi79 – 846Combined sources
Helixi85 – 9511Combined sources
Beta strandi96 – 1016Combined sources
Beta strandi103 – 1053Combined sources
Helixi108 – 1169Combined sources
Beta strandi119 – 1224Combined sources
Beta strandi140 – 1478Combined sources
Turni149 – 1513Combined sources
Helixi157 – 1659Combined sources
Beta strandi169 – 1735Combined sources
Helixi177 – 1804Combined sources
Helixi185 – 1895Combined sources
Beta strandi192 – 2009Combined sources
Turni201 – 2044Combined sources
Helixi207 – 2093Combined sources
Beta strandi212 – 2165Combined sources
Helixi218 – 22710Combined sources
Helixi235 – 24612Combined sources
Helixi248 – 27225Combined sources
Beta strandi281 – 2877Combined sources
Helixi291 – 30212Combined sources
Beta strandi305 – 3106Combined sources
Beta strandi313 – 3175Combined sources
Helixi321 – 33212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H1CX-ray2.85A/B/C/D1-335[»]
1UU0X-ray2.85A/B/C/D1-335[»]
1UU1X-ray2.38A/B/C/D1-335[»]
1UU2X-ray2.80A/B1-335[»]
2F8JX-ray2.40A/B/C/D1-335[»]
ProteinModelPortaliQ9X0D0.
SMRiQ9X0D0. Positions 1-335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X0D0.

Family & Domainsi

Sequence similaritiesi

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CIH. Bacteria.
COG0079. LUCA.
InParanoidiQ9X0D0.
KOiK00817.
OMAiSCYRIFA.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01023. HisC_aminotrans_2. 1 hit.
InterProiIPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR005861. HisP_aminotrans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01141. hisC. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9X0D0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPLDLIAKR AYPYETEKRD KTYLALNENP FPFPEDLVDE VFRRLNSDAL
60 70 80 90 100
RIYYDSPDEE LIEKILSYLD TDFLSKNNVS VGNGADEIIY VMMLMFDRSV
110 120 130 140 150
FFPPTYSCYR IFAKAVGAKF LEVPLTKDLR IPEVNVGEGD VVFIPNPNNP
160 170 180 190 200
TGHVFEREEI ERILKTGAFV ALDEAYYEFH GESYVDFLKK YENLAVIRTF
210 220 230 240 250
SKAFSLAAQR VGYVVASEKF IDAYNRVRLP FNVSYVSQMF AKVALDHREI
260 270 280 290 300
FEERTKFIVE ERERMKSALR EMGYRITDSR GNFVFVFMEK EEKERLLEHL
310 320 330
RTKNVAVRSF REGVRITIGK REENDMILRE LEVFK
Length:335
Mass (Da):39,298
Last modified:November 1, 1999 - v1
Checksum:iD7CA1B807825376A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36117.1.
PIRiG72304.
RefSeqiNP_228846.1. NC_000853.1.
WP_004080482.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD36117; AAD36117; TM_1040.
GeneIDi897350.
KEGGitma:TM1040.
tmi:THEMA_09160.
tmw:THMA_1062.
PATRICi23937009. VBITheMar51294_1053.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36117.1.
PIRiG72304.
RefSeqiNP_228846.1. NC_000853.1.
WP_004080482.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H1CX-ray2.85A/B/C/D1-335[»]
1UU0X-ray2.85A/B/C/D1-335[»]
1UU1X-ray2.38A/B/C/D1-335[»]
1UU2X-ray2.80A/B1-335[»]
2F8JX-ray2.40A/B/C/D1-335[»]
ProteinModelPortaliQ9X0D0.
SMRiQ9X0D0. Positions 1-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1040.

Protocols and materials databases

DNASUi897350.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36117; AAD36117; TM_1040.
GeneIDi897350.
KEGGitma:TM1040.
tmi:THEMA_09160.
tmw:THMA_1062.
PATRICi23937009. VBITheMar51294_1053.

Phylogenomic databases

eggNOGiENOG4105CIH. Bacteria.
COG0079. LUCA.
InParanoidiQ9X0D0.
KOiK00817.
OMAiSCYRIFA.

Enzyme and pathway databases

UniPathwayiUPA00031; UER00012.
BRENDAi2.6.1.9. 6331.
SABIO-RKQ9X0D0.

Miscellaneous databases

EvolutionaryTraceiQ9X0D0.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_01023. HisC_aminotrans_2. 1 hit.
InterProiIPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR005861. HisP_aminotrans.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01141. hisC. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHIS8_THEMA
AccessioniPrimary (citable) accession number: Q9X0D0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: November 1, 1999
Last modified: September 7, 2016
This is version 119 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

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.