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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Rhodococcus jostii (strain RHA1)
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)
  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:RHA1_ro01030
OrganismiRhodococcus jostii (strain RHA1)
Taxonomic identifieri101510 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesNocardiaceaeRhodococcus
Proteomesi
  • UP000008710 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000634981 – 380Histidinol-phosphate aminotransferaseAdd BLAST380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei235N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PRIDEiQ0SHX9.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi101510.RHA1_ro01030.

Structurei

3D structure databases

ProteinModelPortaliQ0SHX9.
SMRiQ0SHX9.
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.

Q0SHX9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAANVPGSS IGVDALPIRE NLRGKSAYGA PQLTVPVQLN TNENPHPPTK
60 70 80 90 100
ALVDDVAESV REAARELHRY PDRDAVALRT DLAAYLVRQT GVPVTVDNVW
110 120 130 140 150
AANGSNEILQ QLLQAFGGPG RSAMGFVPSY SMHPIIADGT ETEWLPIFRR
160 170 180 190 200
ADFALDVDAA TAAITERRPD VVFVTSPNNP TGHSVGIAEL RRVLDAAPGI
210 220 230 240 250
VIVDEAYAEF SDAPSALTLI DEYPSKLVVS RTMSKAFAFA GGRLGYLAAA
260 270 280 290 300
PAFIEALLLV RLPYHLSVVT QAAARAALRH ANETLASVHA LATERVRVSK
310 320 330 340 350
ALDDTGFRVI PSDANFILFG EFTDSAHAWR AYLDRGVLIR DVGIPGYLRA
360 370 380
TVGLASENDA FIVASDEIAA TELTSSGDRG
Length:380
Mass (Da):40,594
Last modified:September 5, 2006 - v1
Checksum:iD5296DA0737EFC6E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000431 Genomic DNA. Translation: ABG92857.1.
RefSeqiWP_011594185.1. NC_008268.1.

Genome annotation databases

EnsemblBacteriaiABG92857; ABG92857; RHA1_ro01030.
GeneIDi4219268.
KEGGirha:RHA1_ro01030.
PATRICifig|101510.16.peg.1050.

Similar proteinsi

Entry informationi

Entry nameiHIS8_RHOJR
AccessioniPrimary (citable) accession number: Q0SHX9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 5, 2006
Last modified: June 7, 2017
This is version 75 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