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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Magnetospirillum magneticum (strain AMB-1 / ATCC 700264)
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 HisH (hisH), Imidazole glycerol phosphate synthase subunit HisF (hisF)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  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 aminotransferaseUniRule annotation (EC:2.6.1.9UniRule annotation)
Alternative name(s):
Imidazole acetol-phosphate transaminaseUniRule annotation
Gene namesi
Name:hisCUniRule annotation
Ordered Locus Names:amb3974
OrganismiMagnetospirillum magneticum (strain AMB-1 / ATCC 700264)
Taxonomic identifieri342108 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeMagnetospirillum
Proteomesi
  • UP000007058 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003197711 – 363Histidinol-phosphate aminotransferaseAdd BLAST363

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei220N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi342108.amb3974.

Structurei

3D structure databases

ProteinModelPortaliQ2W047.
SMRiQ2W047.
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.
OMAiHGFLVYR.
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.

Q2W047-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAPAPRPGI MDIRPYVGGE SAIEGVDRIL KLSSNEGALG PSPKAMEALR
60 70 80 90 100
AMAPEMHRYP DGGAEDLRKA IGARFGLDAS RIVCGAGSDE LLGILCRAYA
110 120 130 140 150
GPGDEVLYSA HGFLMYAIAA KACGATPVTA PEVDLTANVD NLLAAVTPRT
160 170 180 190 200
KILFLANPNN PTGTYLPATE VARLRAGLRA DILLVIDAAY TEFVSRNDYS
210 220 230 240 250
GGIELVEAGD NVVVCRTFSK MYALGGLRLG WAYCPENVAG VLNRVRNPFN
260 270 280 290 300
VGAPALAAGL AAFNDTAYAE LCKSHNDYWL PWLSGQLAEL GLTVVPSVCN
310 320 330 340 350
FILVRFPKDA GKDAGAADKF LRSKGIIVRA MGGYGLGDCL RITIGTGEEN
360
QLVVAALKEF VGA
Length:363
Mass (Da):38,250
Last modified:January 10, 2006 - v1
Checksum:i0E673E16AB26FE12
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007255 Genomic DNA. Translation: BAE52778.1.
RefSeqiWP_011386328.1. NC_007626.1.

Genome annotation databases

EnsemblBacteriaiBAE52778; BAE52778; amb3974.
KEGGimag:amb3974.

Similar proteinsi

Entry informationi

Entry nameiHIS8_MAGSA
AccessioniPrimary (citable) accession number: Q2W047
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: January 10, 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