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Protein

Histidinol-phosphate aminotransferase 2

Gene

hisC2

Organism
Bacillus thuringiensis subsp. konkukian (strain 97-27)
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. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (hisA)
  5. Imidazole glycerol phosphate synthase subunit HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase 2 (hisC2), Histidinol-phosphate aminotransferase 1 (hisC1)
  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 aminotransferase 2UniRule annotation (EC:2.6.1.9UniRule annotation)
Alternative name(s):
Imidazole acetol-phosphate transaminase 2UniRule annotation
Gene namesi
Name:hisC2UniRule annotation
Ordered Locus Names:BT9727_2696
OrganismiBacillus thuringiensis subsp. konkukian (strain 97-27)
Taxonomic identifieri281309 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000001301 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001533111 – 366Histidinol-phosphate aminotransferase 2Add BLAST366

Amino acid modifications

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

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ6HHF6.
SMRiQ6HHF6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000288510.
KOiK00817.
OMAiHGFLVYR.

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.

Q6HHF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVKDQLSSL QPYKPGKSPE QMKEVYGDHS FVKLASNENP FGCSPRVLDE
60 70 80 90 100
LQKSWLDHAL YPDGGATTLR QTIANKLHVK MEQVLCGSGL DEVIQMISRA
110 120 130 140 150
VLKAGDNIVT AEATFPQYRH HAIIEGCEVK EVALNNGVYD LDEISSVVDN
160 170 180 190 200
NTKIVWICNP NNPTGTYVND RKLTQFIEGI SENTLIVIDE AYYEYVTAKD
210 220 230 240 250
FPETLPLLEK HKNILVLRTF SKAYGLASFR IGYAIGQEEL IEKLNVVRLP
260 270 280 290 300
FNVSSLAQKA ATIAFGDDEF IEEIVRVNTE GLRQYESFCK ENEIPFYQSQ
310 320 330 340 350
TNFIFLPVEN GGEIYEACAH AGFIIRPFPN GVRITVGTRE QNEGVISVLQ
360
QHFENKKRKS RDEANA
Length:366
Mass (Da):41,202
Last modified:July 19, 2004 - v1
Checksum:i2E9C0DA0A4E73B1E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017355 Genomic DNA. Translation: AAT61254.1.
RefSeqiWP_001197241.1. NC_005957.1.
YP_037020.1. NC_005957.1.

Genome annotation databases

EnsemblBacteriaiAAT61254; AAT61254; BT9727_2696.
GeneIDi2854919.
KEGGibtk:BT9727_2696.
PATRICifig|281309.8.peg.2862.

Similar proteinsi

Entry informationi

Entry nameiHIS82_BACHK
AccessioniPrimary (citable) accession number: Q6HHF6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: July 19, 2004
Last modified: June 7, 2017
This is version 80 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

Documents

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