Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Methanococcus maripaludis (strain C7 / ATCC BAA-1331)
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. 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:MmarC7_0463
OrganismiMethanococcus maripaludis (strain C7 / ATCC BAA-1331)
Taxonomic identifieri426368 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
Proteomesi
  • UP000002298 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003197991 – 371Histidinol-phosphate aminotransferaseAdd BLAST371

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei228N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Protein-protein interaction databases

STRINGi426368.MmarC7_0463.

Structurei

3D structure databases

ProteinModelPortaliA6VGF6.
SMRiA6VGF6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG04273. Archaea.
COG0079. LUCA.
HOGENOMiHOG000288510.
KOiK00817.
OMAiTYGMYKV.
OrthoDBiPOG093Z043N.

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.

A6VGF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIDDKVRAI VKEFKAYVPG KSKEEIARNY GIDPEKIIKL GSNENPWGCS
60 70 80 90 100
PKIAEKLMDE VSKLHQYPQP INPELMDEIS KFTKMPVENI IVGGDGADEV
110 120 130 140 150
IDNIMRILID EGDEVIIPIP TFTQYAISAK IHGANIKWAK FDEENEFKLD
160 170 180 190 200
IESVLNNITE KTKAIFLCTP NNPTGNVIPT EDIKKIVEST DALVMIDHAY
210 220 230 240 250
IEYSNEDYDL TDWALKYDNV LVLRTFSKVF GLAGQRVGYG VTSKKIVDYM
260 270 280 290 300
MRIKPIFSLT RASQASAITA LQDKEFFEKC LNEGIESREE IYNGLKKFKQ
310 320 330 340 350
LEVYPTEANY MLVKVKNGMN SSEFCEVLLK KGVIVRDCYS FEGLEPYYFR
360 370
VSIGTFDENE RFLKIMSEVV E
Length:371
Mass (Da):42,295
Last modified:August 21, 2007 - v1
Checksum:iF4E3BBA41CE34EC1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000745 Genomic DNA. Translation: ABR65532.1.
RefSeqiWP_011976864.1. NC_009637.1.

Genome annotation databases

EnsemblBacteriaiABR65532; ABR65532; MmarC7_0463.
GeneIDi5329517.
KEGGimmz:MmarC7_0463.

Similar proteinsi

Entry informationi

Entry nameiHIS8_METM7
AccessioniPrimary (citable) accession number: A6VGF6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 2007
Last modified: June 7, 2017
This is version 65 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

Documents

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