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Protein

Histidinol-phosphate aminotransferase 2

Gene

hisC2

Organism
Bacillus cereus (strain ATCC 10987 / NRS 248)
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 (hisG), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  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 1 (hisC1), Histidinol-phosphate aminotransferase 2 (hisC2)
  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:BCE_2996
OrganismiBacillus cereus (strain ATCC 10987 / NRS 248)
Taxonomic identifieri222523 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000002527 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001533001 – 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

ProteinModelPortaliQ736A5.
SMRiQ736A5.
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.

Q736A5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVKDQLSSL QPYKPGKSPE QMKEVYGDHA FVKLASNENP FGCSPRVLDE
60 70 80 90 100
LQKSWLDHAL YPDGGATTLR QTIANKLQVQ MEQVLCGSGL DEVIQIISRA
110 120 130 140 150
ALKAGDNIVT AGATFPQYRH HAIIEGCEVK EVPLNNGVYD LDEISSAVNN
160 170 180 190 200
NTKIVWICNP NNPTGTYVND RKLTQFIEGI SENTLIVIDE AYYEYVTAKD
210 220 230 240 250
FPETLPLLEK HKNILVLRTF SKAYGLASFR VGYAIGQEEL IEKLNVVRLP
260 270 280 290 300
FNVSSLAQKA ATIAFGDDEF IEEIVRVNTE GLQQYESFCK ENDIPFYPSQ
310 320 330 340 350
TNFIFLPVEN AGEIYEACAH AGFIIRPFPN GVRITVGTRE QNEGVISVLQ
360
QHFENKKRKS RDEANA
Length:366
Mass (Da):40,982
Last modified:July 5, 2004 - v1
Checksum:i7E12832B79B95583
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS41907.1.
RefSeqiWP_001197235.1. NC_003909.8.

Genome annotation databases

EnsemblBacteriaiAAS41907; AAS41907; BCE_2996.
KEGGibca:BCE_2996.

Similar proteinsi

Entry informationi

Entry nameiHIS82_BACC1
AccessioniPrimary (citable) accession number: Q736A5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: July 5, 2004
Last modified: June 7, 2017
This is version 82 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