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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Rhodobacter sphaeroides (strain KD131 / KCTC 12085)
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 (RSKD131_3717)
  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 (hisC)
  8. no protein annotated in this organism
  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

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:RSKD131_0607
OrganismiRhodobacter sphaeroides (strain KD131 / KCTC 12085)
Taxonomic identifieri557760 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000001597 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001491111 – 361Histidinol-phosphate aminotransferaseAdd BLAST361

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei219N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB9KPH4.
SMRiB9KPH4.
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
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.

B9KPH4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDAIRPQPG ILDIALYEGG KSHVAGIQNA LKLSSNENPF GPSPKAKEAF
60 70 80 90 100
LRSVHTLHRY PSTDHAGLRH AIAEVHGLDP ARVICGVGSD EIITFLCQAY
110 120 130 140 150
AGPHTDVVFT EHGFLMYRIS ALAVGANPVE VPERERTTDV DAILAACTPH
160 170 180 190 200
TRLVFLANPN NPTGTMIGQA DLARLAAGLP AQAILVLDGA YAEYVPGYDA
210 220 230 240 250
GLALIEERGN VVMTRTFSKI YGLGGLRVGW GYGPKSIIDV LNRIRGPFNL
260 270 280 290 300
STTQLETAEA AVRDQDHVAR CRADNARWRI WLAEALAEIG VPSDTSMANF
310 320 330 340 350
ILARFSDTEE AEACDLHLQT QGLIVRRVAG YKLPHCLRIT IGDEASCRRV
360
AHAIGQFKRM R
Length:361
Mass (Da):39,179
Last modified:March 24, 2009 - v1
Checksum:i911DF7E157DCFAAD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001150 Genomic DNA. Translation: ACM00467.1.
RefSeqiWP_012643841.1. NC_011963.1.

Genome annotation databases

EnsemblBacteriaiACM00467; ACM00467; RSKD131_0607.
KEGGirsk:RSKD131_0607.

Similar proteinsi

Entry informationi

Entry nameiHIS8_RHOSK
AccessioniPrimary (citable) accession number: B9KPH4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: June 7, 2017
This is version 51 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