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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1)
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 regulatory subunit (hisZ)
  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:Mpe_A0832
OrganismiMethylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1)
Taxonomic identifieri420662 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium
Proteomesi
  • UP000000366 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003197741 – 371Histidinol-phosphate aminotransferaseAdd BLAST371

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei232N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi420662.Mpe_A0832.

Structurei

3D structure databases

ProteinModelPortaliA2SE05.
SMRiA2SE05.
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.

A2SE05-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSNSNNGG PPLAPRLARF VRQDVQNMHA YAIQPSDGFV KLDAMENPHR
60 70 80 90 100
LPAALQAELG RRLGALAINR YPGTRTDELR AALARHAGLP PGCALMLGNG
110 120 130 140 150
SDELISLLSM ACDVPGATVL APLPGFVMYE MSARLQGLRF VGVPLTADFE
160 170 180 190 200
LDAAAMLAAV REHRPALTYL AYPNNPTANL WDDAVIERVV DAVREHGGLV
210 220 230 240 250
VIDEAYQPFA SRSYIDRLAH HDHVLLMRTL SKFGLAGVRL GYLMGPTALV
260 270 280 290 300
AEIDKVRPPY NVSVLNCEAA LFALEHEDEF ARQAAVLRAE RARLLDALRA
310 320 330 340 350
MSGATPFPSE ANMVLVRVPD AKAAFEGLKA RGVLVKNVSG LHPLLANCLR
360 370
LTVGLPEEND QMIAALKGIL S
Length:371
Mass (Da):40,030
Last modified:March 6, 2007 - v1
Checksum:i813CECE18D0F9260
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000555 Genomic DNA. Translation: ABM93794.1.
RefSeqiWP_011828432.1. NC_008825.1.

Genome annotation databases

EnsemblBacteriaiABM93794; ABM93794; Mpe_A0832.
KEGGimpt:Mpe_A0832.

Similar proteinsi

Entry informationi

Entry nameiHIS8_METPP
AccessioniPrimary (citable) accession number: A2SE05
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 6, 2007
Last modified: June 7, 2017
This is version 68 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