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Protein

Histidinol-phosphate aminotransferase

Gene

hisC

Organism
Cyanothece sp. (strain PCC 7425 / ATCC 29141)
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), ATP phosphoribosyltransferase regulatory subunit (hisZ)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Histidine biosynthesis bifunctional protein HisIE (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:Cyan7425_2316
OrganismiCyanothece sp. (strain PCC 7425 / ATCC 29141)
Taxonomic identifieri395961 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesCyanothecaceaeCyanothece
Proteomesi
  • UP000002511 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001490911 – 374Histidinol-phosphate aminotransferaseAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei237N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi395961.Cyan7425_2316.

Structurei

3D structure databases

ProteinModelPortaliB8HW95.
SMRiB8HW95.
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.

Sequencei

Sequence statusi: Complete.

B8HW95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPFLRSELA GLTAYVPHPE ADADGAAARG LDRLDANEFP LDLPEDLKQK
60 70 80 90 100
LAWSYQQELE ANRYPDGGHW ELKRAIAEYV NEALPVPSWI DHSHVSIGNG
110 120 130 140 150
SDELIRSLLI TTCLNQQGAI LVAEPTFSMY RITAETLGIP VVAVGRNPDT
160 170 180 190 200
FEIDCSAAQA AIEATEQNRP PIRVVFVVHP NSPTGNGLTI AEQEWLRTLP
210 220 230 240 250
PDILVVIDEA YFEFCRSTLA GEIVQRSNWI ILRTFSKAFR LAAHRVGYAI
260 270 280 290 300
AGPELIAVLE KIRLPYNLPA YSQLAAQLAL SQRQSLLAEI ELIWQERNRL
310 320 330 340 350
FQALAPIPDL RLWPSAANFI YVQMSTEAAT AQLGRDLKAL GTSIRYTGGG
360 370
LRISVGTVAE NDRTLERIHR LLAK
Length:374
Mass (Da):41,465
Last modified:March 3, 2009 - v1
Checksum:i76FA63EA9A5D93C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001344 Genomic DNA. Translation: ACL44674.1.
RefSeqiWP_012627749.1. NC_011884.1.

Genome annotation databases

EnsemblBacteriaiACL44674; ACL44674; Cyan7425_2316.
KEGGicyn:Cyan7425_2316.

Similar proteinsi

Entry informationi

Entry nameiHIS8_CYAP4
AccessioniPrimary (citable) accession number: B8HW95
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: June 7, 2017
This is version 45 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