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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)DescriptionActionsGraphical viewLength
ChainiPRO_00001534701 – 335Histidinol-phosphate aminotransferaseAdd BLAST335

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei202N6-(pyridoxal phosphate)lysine1

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi243274.TM1040.

Structurei

Secondary structure

1335
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 5Combined sources4
Beta strandi21 – 26Combined sources6
Helixi35 – 43Combined sources9
Helixi47 – 51Combined sources5
Helixi59 – 69Combined sources11
Helixi76 – 78Combined sources3
Beta strandi79 – 84Combined sources6
Helixi85 – 95Combined sources11
Beta strandi96 – 101Combined sources6
Beta strandi103 – 105Combined sources3
Helixi108 – 116Combined sources9
Beta strandi119 – 122Combined sources4
Beta strandi140 – 147Combined sources8
Turni149 – 151Combined sources3
Helixi157 – 165Combined sources9
Beta strandi169 – 173Combined sources5
Helixi177 – 180Combined sources4
Helixi185 – 189Combined sources5
Beta strandi192 – 200Combined sources9
Turni201 – 204Combined sources4
Helixi207 – 209Combined sources3
Beta strandi212 – 216Combined sources5
Helixi218 – 227Combined sources10
Helixi235 – 246Combined sources12
Helixi248 – 272Combined sources25
Beta strandi281 – 287Combined sources7
Helixi291 – 302Combined sources12
Beta strandi305 – 310Combined sources6
Beta strandi313 – 317Combined sources5
Helixi321 – 332Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
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
PDB 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.
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.
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: November 2, 2016
This is version 121 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.