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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: -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

Keywordsi

Molecular functionAminotransferase, Transferase
Biological processAmino-acid biosynthesis, Histidine biosynthesis
LigandPyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.6.1.9 6331
SABIO-RKiQ9X0D0
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

Pathology & Biotechi

Chemistry databases

DrugBankiDB03997 Phosphoric Acid Mono-[2-Amino-3-(3h-Imidazol-4-Yl)-Propyl]Ester
DB02142 Pyridoxamine-5'-Phosphate

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

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
OMAiPTFDGYP

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
HAMAPiMF_01023 HisC_aminotrans_2, 1 hit
InterProiView protein in InterPro
IPR001917 Aminotrans_II_pyridoxalP_BS
IPR004839 Aminotransferase_I/II
IPR005861 HisP_aminotrans
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00155 Aminotran_1_2, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR01141 hisC, 1 hit
PROSITEiView protein in PROSITE
PS00599 AA_TRANSFER_CLASS_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiHIS8_THEMA
AccessioniPrimary (citable) accession number: Q9X0D0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: November 1, 1999
Last modified: April 25, 2018
This is version 127 of the entry and version 1 of the sequence. See 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

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