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P45358 (HIS8_ACEPA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Histidinol-phosphate aminotransferase

EC=2.6.1.9
Alternative name(s):
Imidazole acetol-phosphate transaminase
Gene names
Name:hisC
Synonyms:his1
OrganismAcetobacter pasteurianus (Acetobacter turbidans)
Taxonomic identifier438 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcetobacter

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. HAMAP MF_01023

Cofactor

Pyridoxal phosphate By similarity. HAMAP MF_01023

Pathway

Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. HAMAP MF_01023

Subunit structure

Homodimer By similarity. HAMAP MF_01023

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Histidinol-phosphate aminotransferase HAMAP MF_01023
PRO_0000153290

Amino acid modifications

Modified residue2101N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P45358 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 8926199C5242DF51

FASTA35639,136
        10         20         30         40         50         60 
MSRFWSPLVH KLTPYVPGEQ PKMTDLIKLN TNESPYGPSP RALEAIRAAD NDTLRLYPDP 

        70         80         90        100        110        120 
EALALRKALG ARIGLGPEYV FVGNGSDEVL AHAFQAFFAH GEPLLFPDVT YSFYKVYCGL 

       130        140        150        160        170        180 
YSLPFRNVPL TDDMQVNVAD YAGPCSGVVV ANPNAPTGIA LDLADVRKLL ELQPNRVVLI 

       190        200        210        220        230        240 
DEAYVDFGAE SAVSLIKEYP NLLVVQTFSK SRALAGLRVG FAFGQPELIE GLVRIKDSFN 

       250        260        270        280        290        300 
SYPLDRLAQV GATAAVEDEA WLATSVQKVM ASRTVLTEGL QKLGFDVLPS KANFVYTRHP 

       310        320        330        340        350 
NRNAAELATQ LRERAIIVRH LRGERTAAWL RITVGTDQQC ETLLSALRDI LCSNSL 

« Hide

References

[1]"Suppression of an ethanol-sensitive mutation of Acetobacter pasteurianus by overexpression of the his1 gene encoding histidinol phosphate aminotransferase."
Takemura H., Horinouchi S., Beppu T.
J. Ferment. Bioeng. 76:224-228(1993)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NCI 1452.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14440 Genomic DNA. Translation: BAA03332.1.
PIRI39488.

3D structure databases

ProteinModelPortalP45358.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_01023. HisC_aminotrans_2.
[Tree]
InterProIPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR005861. HisP_aminotrans.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01141. HisC. 1 hit.
PROSITEPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHIS8_ACEPA
AccessionPrimary (citable) accession number: P45358
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 16, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families