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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Methanococcus maripaludis (strain S2 / LL)
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 HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH 2 (hisH2), Imidazole glycerol phosphate synthase subunit HisH 1 (hisH1)
  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:MMP1216
OrganismiMethanococcus maripaludis (strain S2 / LL)
Taxonomic identifieri267377 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
Proteomesi
  • UP000000590 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001535001 – 371Histidinol-phosphate aminotransferaseAdd BLAST371

Amino acid modifications

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

Interactioni

Protein-protein interaction databases

STRINGi267377.MMP1216.

Structurei

3D structure databases

ProteinModelPortaliP61003.
SMRiP61003.
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.

P61003-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIDDKVRSI VKEFKAYVPG KSKEEIARNY GIDPERIIKL GSNENPWGCS
60 70 80 90 100
PKIEEKLLNE VSNLHQYPQP INPELMDEIS KFTKMPVENI IVGGDGADEV
110 120 130 140 150
IDNIMRILID EGDEVIIPIP TFTQYAISAK IHGANIKWAK FDEENGFKLD
160 170 180 190 200
VESVLNNITE KTKAIFLCTP NNPTGNVIPT EDIKKIVEST DALVMIDHAY
210 220 230 240 250
IEYSKEEYDL TSWALKYDNV LVLRTFSKVF GLAGQRVGYG VTSKKVVDYM
260 270 280 290 300
MRIKPIFSLT RASQVSAITA LQDKEFFEKC LKEGIESREE IYNGLKKFKQ
310 320 330 340 350
LEVYPTEANY MLVKVKNGMN SSEFCEALLK KGVIVRDCYS FEGLEPYYFR
360 370
VSIGTSEENE RFLKIMSEIV E
Length:371
Mass (Da):42,246
Last modified:April 26, 2004 - v1
Checksum:i60D0EEDEF1F3C9F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX950229 Genomic DNA. Translation: CAF30772.1.
RefSeqiWP_011171160.1. NC_005791.1.

Genome annotation databases

EnsemblBacteriaiCAF30772; CAF30772; MMP1216.
GeneIDi2761452.
KEGGimmp:MMP1216.
PATRICifig|267377.15.peg.1249.

Similar proteinsi

Entry informationi

Entry nameiHIS8_METMP
AccessioniPrimary (citable) accession number: P61003
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: June 7, 2017
This is version 80 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