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Protein

Histidinol-phosphate aminotransferase 2

Gene

hisC2

Organism
Anabaena variabilis (strain ATCC 29413 / PCC 7937)
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 regulatory subunit (hisZ), ATP phosphoribosyltransferase (hisG)
  2. Histidine biosynthesis bifunctional protein HisIE (hisI)
  3. Phosphoribosyl-AMP cyclohydrolase (hisI), 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 HisF (hisF), Imidazole glycerol phosphate synthase subunit HisH (hisH)
  6. Imidazoleglycerol-phosphate dehydratase (hisB)
  7. Histidinol-phosphate aminotransferase 1 (hisC1), Histidinol-phosphate aminotransferase 2 (hisC2)
  8. no protein annotated in this organism
  9. Histidinol dehydrogenase 1 (hisD1), Histidinol dehydrogenase 2 (hisD2)
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

BioCyciAVAR240292:G7WH-10608-MONOMER.
UniPathwayiUPA00031; UER00012.

Names & Taxonomyi

Protein namesi
Recommended name:
Histidinol-phosphate aminotransferase 2UniRule annotation (EC:2.6.1.9UniRule annotation)
Alternative name(s):
Imidazole acetol-phosphate transaminase 2UniRule annotation
Gene namesi
Name:hisC2UniRule annotation
Ordered Locus Names:Ava_2242
OrganismiAnabaena variabilis (strain ATCC 29413 / PCC 7937)
Taxonomic identifieri240292 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeTrichormus
Proteomesi
  • UP000002533 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002302021 – 380Histidinol-phosphate aminotransferase 2Add BLAST380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei236N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PRIDEiQ3MAX6.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi240292.Ava_2242.

Structurei

3D structure databases

ProteinModelPortaliQ3MAX6.
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.

Q3MAX6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPFIRSDLA QFTAYKPHPS SDTDAAVPAQ LDRLDTNESP CDLPPELKQK
60 70 80 90 100
LAWTFQQVIE SNRYPDGGHE ELKDAIAQYV NESANISSSP ITAANISVGN
110 120 130 140 150
GSDELIRSLL IATCLGAQGS ILVANPTFSM YGILAQTLGI PVVTVSRNPE
160 170 180 190 200
NFEIDLTAAQ SAIEQTQNPP IRVVFVVHPN SPTANPLTTN ELRWLKSLSE
210 220 230 240 250
QILVVVDEAY FEFSQTTLIS ELVQRPNWVI LRTFSKAFRL AAMRVGYCVA
260 270 280 290 300
HPEAIAILEK VRLPYNLPSF SITSALVALQ NRAILLESIP QILNERAKLI
310 320 330 340 350
TALSKYPELA VAESAANFIF LQLKTDNKNS PDTALLNLHQ QLKNSGTLVR
360 370 380
QISGGLRITI GTPEENIRTL NHIQTALIKA
Length:380
Mass (Da):41,730
Last modified:October 25, 2005 - v1
Checksum:i97124B9B0046E6C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000117 Genomic DNA. Translation: ABA21860.1.

Genome annotation databases

EnsemblBacteriaiABA21860; ABA21860; Ava_2242.
KEGGiava:Ava_2242.

Similar proteinsi

Entry informationi

Entry nameiHIS82_ANAVT
AccessioniPrimary (citable) accession number: Q3MAX6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 25, 2005
Last modified: November 22, 2017
This is version 69 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