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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Baumannia cicadellinicola subsp. Homalodisca coagulata
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. 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 HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Histidine biosynthesis bifunctional protein HisB (hisB)
  7. Histidinol-phosphate aminotransferase (hisC)
  8. Histidine biosynthesis bifunctional protein HisB (hisB)
  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:BCI_0403
OrganismiBaumannia cicadellinicola subsp. Homalodisca coagulata
Taxonomic identifieri374463 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia
Proteomesi
  • UP000002427 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000634631 – 360Histidinol-phosphate aminotransferaseAdd BLAST360

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei213N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PRIDEiQ1LT68.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi374463.BCI_0403.

Structurei

3D structure databases

ProteinModelPortaliQ1LT68.
SMRiQ1LT68.
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.
HOGENOMiHOG000288512.
KOiK00817.
OMAiTYGMYKV.
OrthoDBiPOG091H05S1.

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.

Q1LT68-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSILNLARTN VLTLEPYQSA RRIGGGSQGN IWLNANEYPQ PTFYMLRSSN
60 70 80 90 100
LNRYPDCQPQ ELLNSYAAYA GVQPNQVLAC RGADEGIELL IRTFCEPSKD
110 120 130 140 150
KILFCPPTYG MYRVSAETFG VAYCAIQALD NWQLDLDTIY AQLDCVKLIY
160 170 180 190 200
ICHPNNPTGN IINPSDIRQL LDITHGRTIL VVDEAYIDFY PTASISSWIN
210 220 230 240 250
HYPHLVILRT LSKAFALAGL RCGFILANPD IIKLLLKVIA PYPISRPVVD
260 270 280 290 300
IAKQALSTKG IHQTKRRVAN IDINRNWLIQ QLAECSCVSV VFPSVTNYLL
310 320 330 340 350
VRFHPNYHVF QSLWKKGTIL RDQNQQIGLA NCLRITIGTS LECQNLLTAL
360
QALTLVSHKE
Length:360
Mass (Da):40,496
Last modified:May 30, 2006 - v1
Checksum:i7CF6EB03501FD99E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000238 Genomic DNA. Translation: ABF14107.1.
RefSeqiWP_011520579.1. NC_007984.1.

Genome annotation databases

EnsemblBacteriaiABF14107; ABF14107; BCI_0403.
KEGGibci:BCI_0403.

Similar proteinsi

Entry informationi

Entry nameiHIS8_BAUCH
AccessioniPrimary (citable) accession number: Q1LT68
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 30, 2006
Last modified: June 7, 2017
This is version 76 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