Tag | Content |
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CPLM ID | CPLM-013889 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Phosphoenolpyruvate carboxykinase [ATP] |
Protein Synonyms/Alias | PEP carboxykinase; PEPCK; Phosphoenolpyruvate carboxylase |
Gene Name | pckA |
Gene Synonyms/Alias | tthHB8IM; TTHA0278 |
Created Date | July 27, 2013 |
Organism | Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) |
NCBI Taxa ID | 300852 |
Lysine Modification | Position | Peptide | Type | References |
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413 | YARMLGEKIRKHAPR | acetylation | [1] | 512 | LFQENFQKYASGVAK | acetylation | [1] |
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Reference | [1] Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus. Okanishi H, Kim K, Masui R, Kuramitsu S. J Proteome Res. 2013 Aug 1;. [ PMID: 23901841] |
Functional Description | |
Sequence Annotation | NP_BIND 232 239 ATP. METAL 130 130 Calcium; via carbonyl oxygen. METAL 131 131 Calcium; via carbonyl oxygen. METAL 133 133 Calcium; via carbonyl oxygen. METAL 267 267 Calcium; via carbonyl oxygen. BINDING 439 439 ATP; via carbonyl oxygen. BINDING 444 444 ATP. |
Keyword | 3D-structure; ATP-binding; Calcium; Complete proteome; Cytoplasm; Decarboxylase; Gluconeogenesis; Lyase; Metal-binding; Nucleotide-binding; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 529 AA |
Protein Sequence | MQRLEALGIH PKKRVFWNTV SPVLVEHTLL RGEGLLAHHG PLVVDTTPYT GRSPKDKFVV 60 REPEVEGEIW WGEVNQPFAP EAFEALYQRV VQYLSERDLY VQDLYAGADR RYRLAVRVVT 120 ESPWHALFAR NMFILPRRFG NDDEVEAFVP GFTVVHAPYF QAVPERDGTR SEVFVGISFQ 180 RRLVLIVGTK YAGEIKKSIF TVMNYLMPKR GVFPMHASAN VGKEGDVAVF FGLSGTGKTT 240 LSTDPERPLI GDDEHGWSED GVFNFEGGCY AKVIRLSPEH EPLIYKASNQ FEAILENVVV 300 NPESRRVQWD DDSKTENTRS SYPIAHLENV VESGVAGHPR AIFFLSADAY GVLPPIARLS 360 PEEAMYYFLS GYTARVAGTE RGVTEPRATF SACFGAPFLP MHPGVYARML GEKIRKHAPR 420 VYLVNTGWTG GPYGVGYRFP LPVTRALLKA ALSGALENVP YRRDPVFGFE VPLEAPGVPQ 480 ELLNPRETWA DKEAYDQQAR KLARLFQENF QKYASGVAKE VAEAGPRTE 529 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005524; F:ATP binding; IEA:HAMAP. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:HAMAP. GO:0006094; P:gluconeogenesis; IEA:HAMAP. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |