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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Geobacillus kaustophilus (strain HTA426)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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 regulatory subunit (hisZ), ATP phosphoribosyltransferase (hisG)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (hisI)
  4. 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)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  9. 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

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:GK2198
OrganismiGeobacillus kaustophilus (strain HTA426)
Taxonomic identifieri235909 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillusGeobacillus thermoleovorans group
Proteomesi
  • UP000001172 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001533631 – 365Histidinol-phosphate aminotransferaseAdd BLAST365

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei222N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PRIDEiQ5KXV3.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi235909.GK2198.

Structurei

3D structure databases

ProteinModelPortaliQ5KXV3.
SMRiQ5KXV3.
ModBaseiSearch...
MobiDBiSearch...

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.
HOGENOMiHOG000288510.
KOiK00817.
OMAiTYGMYKV.
OrthoDBiPOG091H05S1.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
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.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_sub2.
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.

Q5KXV3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVKESLRGL SPYQPGKSIE EVKRQYGLPE IIKLASNENP YGSSPSAKAA
60 70 80 90 100
IAAELDRLAV YPDGCARTLR EKVAKHLGVK ETQLLFGNGS DEVVQILCRA
110 120 130 140 150
FLEPGANTVM AAPTFPQYRH NAIIERAEVR EVPLVDGRHD LEAMLAVIDE
160 170 180 190 200
NTRIVWICNP NNPTGTYVND TELRAFLDRV PRHVLVVVDE AYYEYATAPD
210 220 230 240 250
YPQTVPLLNE YEQLVVMRTF SKAYGLAALR VGYGVASEML IRAVEPAREP
260 270 280 290 300
FNTSTIAQAA AAAALDDQAF IRACVERNRA ELERYYRFCE ENGLKYYPSQ
310 320 330 340 350
TNFLFIDFGL DGDEVFRYLL ERGVIVRSGQ ALGLPTGVRV TVGTKEQNDR
360
VLELVSQLLR EKQLA
Length:365
Mass (Da):40,821
Last modified:February 1, 2005 - v1
Checksum:i062C9C041F0DE6BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000043 Genomic DNA. Translation: BAD76483.1.
RefSeqiWP_011231683.1. NC_006510.1.

Genome annotation databases

EnsemblBacteriaiBAD76483; BAD76483; GK2198.
KEGGigka:GK2198.
PATRICifig|235909.7.peg.2353.

Similar proteinsi

Entry informationi

Entry nameiHIS8_GEOKA
AccessioniPrimary (citable) accession number: Q5KXV3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: February 1, 2005
Last modified: June 7, 2017
This is version 76 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families