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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Buchnera aphidicola subsp. Diuraphis noxia
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 (hisG)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (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 cyclase subunit (ATN01_00515), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase (hisC), Histidinol-phosphate aminotransferase (hisC)
  8. Imidazoleglycerol-phosphate dehydratase (hisB)
  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
OrganismiBuchnera aphidicola subsp. Diuraphis noxia
Taxonomic identifieri118101 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesErwiniaceaeBuchnera

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001533311 – 363Histidinol-phosphate aminotransferaseAdd BLAST363

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei215N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PRIDEiQ84I53.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ84I53.
SMRiQ84I53.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily.UniRule annotation

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
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.

Q84I53-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MINSLIKLAR INVQKLQPYQ SARRIGGQHG DVWLNANESP VSVELSFKKK
60 70 80 90 100
LLNRYPECQP IDLISAYADY VRLSTNQILV TRGADEGIEL LIRAFCESGK
110 120 130 140 150
DAIIYCPPTY DMYRVNAEIY NIKYKEVPTI KNTWQLDLLN IKLNLNSVKL
160 170 180 190 200
IYICNPNNPT GSTCSKKDLF DLLEMTLNTS LVVVDEAYIE FLPKESMTLY
210 220 230 240 250
LKKYPNLVIL RTLSKAFALA GIRCGFVLAQ KEIINILNKI ISPYPISIPT
260 270 280 290 300
ASIALESLHK NYIKLMQNRV LDLNANRVWL INKLKKISSV KKIFQSNTNY
310 320 330 340 350
ILVQFFMSEE IFQMLWEKGI IVRNQDHKIN LKQCLRITVG THLECSRLIE
360
EIKFFSKKYL KGV
Length:363
Mass (Da):41,792
Last modified:June 1, 2003 - v1
Checksum:i40C58A3DA9348A9A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF465530 Genomic DNA. Translation: AAO33045.1.
RefSeqiWP_075433162.1. NZ_CP013259.1.

Similar proteinsi

Entry informationi

Entry nameiHIS8_BUCDN
AccessioniPrimary (citable) accession number: Q84I53
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: April 12, 2017
This is version 59 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families