| Tag | Content |
|---|
| CPLM ID | CPLM-009278 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Histidinol-phosphate aminotransferase |
Protein Synonyms/Alias | Imidazole acetol-phosphate transaminase |
Gene Name | hisC |
Gene Synonyms/Alias | RPA4439 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 197 | AYADYVMKNDYELGI | acetylation | [1] |
|
Reference | [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC. J Biol Chem. 2012 May 4;287(19):15590-601. [ PMID: 22416131] |
Functional Description | |
Sequence Annotation | MOD_RES 221 221 N6-(pyridoxal phosphate)lysine (By |
Keyword | Amino-acid biosynthesis; Aminotransferase; Complete proteome; Histidine biosynthesis; Pyridoxal phosphate; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 365 AA |
Protein Sequence | MSRPVPNPGI LDIAPYTPGK SPVAEPGRKV FKLSANETPF GPSPHAIAAY KSAADHLEDY 60
PEGTSRILRE AIGKAYGLDP DRIICGAGSD EILNLLAHTY LAPGDEAISS QHGFLVYPIA 120
TLANGAKNVV APEKNLTTDV DAMLAAVTPN TKLVWLANPN NPTGTYIPFD EVKRLRAGLP 180
SHVVLVLDAA YADYVMKNDY ELGIELVSTT ENTVLTHTFS KVHGLAALRI GWMFGPANIV 240
DAVNRIRGPF NVSVPAQLAA VAAIQDTGHV ERSRAHTDKW RNTLAEELPK LGLTVTRSVC 300
NFVLIHFPTT KGKTAAEADA FLTQRGLVLR ALNNYGLPHA LRMTIGTDEA NALVLENLRE 360
FMGQP 365 |
Gene Ontology | GO:0004400; F:histidinol-phosphate transaminase activity; IEA:HAMAP. GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:EC. GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. GO:0000105; P:histidine biosynthetic process; IEA:HAMAP. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |