Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712)
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 (Bind_1774)
  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:Bind_0307
OrganismiBeijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712)
Taxonomic identifieri395963 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBeijerinckiaceaeBeijerinckia
Proteomesi
  • UP000001695 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001353851 – 378Histidinol-phosphate aminotransferaseAdd BLAST378

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei231N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi395963.Bind_0307.

Structurei

3D structure databases

ProteinModelPortaliB2IDA4.
SMRiB2IDA4.
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.

B2IDA4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQSGSSPRP SSVRPMPHAG VLGIEPYVPG KSAAPGVAKI HKLSSNETPL
60 70 80 90 100
GPSPEAQKAF AASAEKLALY PDGAATLLRT AIASRHGLDP ARIVCGAGSD
110 120 130 140 150
ELLSLLAAVY LGPGEEGIFT EHGFLVYKIA ILTAGGTPIV VPEKDLTTDV
160 170 180 190 200
DAILAAVTPR TRIVYIANPN NPTGTYLPFA EVKRLATSLP PNVLLVLDAA
210 220 230 240 250
YGEYVTRNDY SAGLELVSTH ENVVMTRTFS KIYGLAALRL GWCYAPLAVA
260 270 280 290 300
DALNRVRGPF NTSGPAIATG VAALADQAHI DRAIAHNETW LSWLGEEIGK
310 320 330 340 350
LGFKVTPSVA NFLLLHFEDQ AEAQAVDAFL SSRGLILRAV ASYGLPNCLR
360 370
LTVGTEEANR LVVDGLKDFC RERMKQRG
Length:378
Mass (Da):40,120
Last modified:June 10, 2008 - v1
Checksum:iDFD6D7EFB37F6D19
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001016 Genomic DNA. Translation: ACB93961.1.
RefSeqiWP_012383319.1. NC_010581.1.

Genome annotation databases

EnsemblBacteriaiACB93961; ACB93961; Bind_0307.
KEGGibid:Bind_0307.

Similar proteinsi

Entry informationi

Entry nameiHIS8_BEII9
AccessioniPrimary (citable) accession number: B2IDA4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: June 7, 2017
This is version 57 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