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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Trichodesmium erythraeum (strain IMS101)
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), Phosphoribosyl-AMP cyclohydrolase (Tery_2490)
  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:Tery_4690
OrganismiTrichodesmium erythraeum (strain IMS101)
Taxonomic identifieri203124 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesMicrocoleaceaeTrichodesmium
Proteomesi
  • UP000008878 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000635091 – 376Histidinol-phosphate aminotransferaseAdd BLAST376

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei230N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi203124.Tery_4690.

Structurei

3D structure databases

ProteinModelPortaliQ10VS0.
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.
OMAiTYGMYKV.
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.

Q10VS0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTFIRSNLN NLKAYTPHSA GSSEILLDRL DTNECPYDLP DNLKQKLAEN
60 70 80 90 100
YQQLIETNRY PDGSHLKLKE AIAKYVNEVT PSANISANNI SVGNGSDELI
110 120 130 140 150
RSLLIVTCVG GEGSILTATP TFSMYSILAQ TLGIPVVNVG RKESNFEIDI
160 170 180 190 200
TAAEDAINHT KNPSIKAIFV VHPNSPTANA LNSQELVWLR SLPDDILVVI
210 220 230 240 250
DEAYFEFSQT SLAEELNQHP NWVILRTFSK AFRLASLRVG YAIAHPEIII
260 270 280 290 300
NLEKVRLPYN LPSFSQAAAQ LVLNHSQHLL SFIPEILRER SKLFATFGEI
310 320 330 340 350
PALKVWKSAA NFLYMRLTDE GLKLMGKSSQ DQSLSSLMQR LKTQGTLIRH
360 370
TGGGLRITIG TSEENQRTVE RIKGIF
Length:376
Mass (Da):41,852
Last modified:August 22, 2006 - v1
Checksum:iDC2CD6F65D2E2B20
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000393 Genomic DNA. Translation: ABG53654.1.
RefSeqiWP_011613971.1. NC_008312.1.

Genome annotation databases

EnsemblBacteriaiABG53654; ABG53654; Tery_4690.
KEGGiter:Tery_4690.

Similar proteinsi

Entry informationi

Entry nameiHIS8_TRIEI
AccessioniPrimary (citable) accession number: Q10VS0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 22, 2006
Last modified: June 7, 2017
This is version 74 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