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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Methanococcus maripaludis (strain S2 / LL)
Status
Reviewed-Annotation score: -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

BioCyciMMAR267377:G1G3S-1255-MONOMER
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, 2 hits
HAMAPiMF_01023 HisC_aminotrans_2, 1 hit
InterProiView protein in InterPro
IPR004839 Aminotransferase_I/II
IPR005861 HisP_aminotrans
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
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: April 25, 2018
This is version 82 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

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