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Protein

Histidinol-phosphate aminotransferase 2

Gene

hisC2

Organism
Burkholderia lata (strain ATCC 17760 / LMG 22485 / NCIMB 9086 / R18194 / 383)
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), ATP phosphoribosyltransferase regulatory subunit (hisZ), ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase (hisG), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE), Phosphoribosyl-ATP pyrophosphatase (hisE), Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI), Phosphoribosyl-AMP cyclohydrolase (hisI), Phosphoribosyl-AMP cyclohydrolase (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), 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 HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB), Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase 3 (hisC3), Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase 1 (hisC1), Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase 2 (hisC2), Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC)
  8. no protein annotated in this organism
  9. Histidinol dehydrogenase (hisD), 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

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:Bcep18194_A6135
OrganismiBurkholderia lata (strain ATCC 17760 / LMG 22485 / NCIMB 9086 / R18194 / 383)
Taxonomic identifieri482957 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
Proteomesi
  • UP000002705 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002302091 – 355Histidinol-phosphate aminotransferase 2Add BLAST355

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei213N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ39CT7.
SMRiQ39CT7.
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.
OMAiVYCGLYG.
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
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.

Sequencei

Sequence statusi: Complete.

Q39CT7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRYWSDIVQ QLVPYVPGEQ PALAHPVKLN TNENPYPPSP RVVAAIAREL
60 70 80 90 100
GETGDTLRRY PDPVARALRE TVATHHRIKP EQVFVGNGSD EVLAHTFQAL
110 120 130 140 150
LKHDRPLRFP DITYSFYPTY ARLYGVQTSN VPLADDFSIR VDDYLDDAGG
160 170 180 190 200
VLFPNPNAPT GRALPLADVE RIVAANPSSV VVIDEAYVDF GAQSAITLID
210 220 230 240 250
RYPNLLVVHT TSKARSLAGM RVGFAFGEAA LIDALNRVKD SFNSYPLDRL
260 270 280 290 300
AQVAAQAAYE DTDYFNATCR RVIDSRTRLT HALDALDFNI VPSAANFVFA
310 320 330 340 350
RHPAHDAGAI AAKLKEREIF VRHFRLPRID QHLRITVGTD AECDALVAAL

RELLA
Length:355
Mass (Da):39,281
Last modified:November 22, 2005 - v1
Checksum:iD9F100AE36CDCF37
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000151 Genomic DNA. Translation: ABB09729.1.
RefSeqiWP_011353237.1. NC_007510.1.

Genome annotation databases

EnsemblBacteriaiABB09729; ABB09729; Bcep18194_A6135.
KEGGibur:Bcep18194_A6135.
PATRICifig|482957.22.peg.3140.

Similar proteinsi

Entry informationi

Entry nameiHIS82_BURL3
AccessioniPrimary (citable) accession number: Q39CT7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 22, 2005
Last modified: June 7, 2017
This is version 71 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