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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Ruegeria sp. (strain TM1040) (Silicibacter sp.)
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 (TM1040_0505)
  2. Phosphoribosyl-ATP pyrophosphatase (hisE)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI)
  4. 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase 1 (hisA1), 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase 2 (hisA2)
  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:TM1040_2101
OrganismiRuegeria sp. (strain TM1040) (Silicibacter sp.)
Taxonomic identifieri292414 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria
Proteomesi
  • UP000000636 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000635011 – 362Histidinol-phosphate aminotransferaseAdd BLAST362

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei218N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi292414.TM1040_2101.

Structurei

3D structure databases

ProteinModelPortaliQ1GET3.
SMRiQ1GET3.
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.

Q1GET3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQITPQPGI MDIALYQGGA AHVDGVSNVT KLSSNENPLG PSPAAVEAMA
60 70 80 90 100
EAAATMHRYP SSDHATLRAA IAETHGLDAE RIICGAGSDE IIAFLCQCYA
110 120 130 140 150
GPGDEVLYTE HGFAMYRISA LAAGATPVEV KERERVTDVD ALLAGCTAQT
160 170 180 190 200
KLVFIANPNN PTGTMISEAE VARLADGIPE DAILVLDGAY AEYVEGFDAG
210 220 230 240 250
AQLIAARHNV VMTRTFSKIY GLGGARVGWA YGPQEIIDVL NRVRGPFNVS
260 270 280 290 300
TTALAGAEAA VRDTDYVQRC RLENAKWRGW LADQLAELGV PSDTSCTNFI
310 320 330 340 350
LARFASQSEA ESCDDFLKQR GLIVRRVAGY NLPTALRITI GDETACRAVA
360
AAVKDFKAGA AE
Length:362
Mass (Da):38,383
Last modified:June 27, 2006 - v1
Checksum:i7E259A0F65CFE1E0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000377 Genomic DNA. Translation: ABF64833.1.
RefSeqiWP_011539425.1. NC_008044.1.

Genome annotation databases

EnsemblBacteriaiABF64833; ABF64833; TM1040_2101.
KEGGisit:TM1040_2101.

Similar proteinsi

Entry informationi

Entry nameiHIS8_RUEST
AccessioniPrimary (citable) accession number: Q1GET3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 27, 2006
Last modified: June 7, 2017
This is version 73 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