Tag | Content |
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CPLM ID | CPLM-026625 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Fructose-bisphosphate aldolase |
Protein Synonyms/Alias | |
Gene Name | cbbA |
Gene Synonyms/Alias | RPA4642 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
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303 | KAEFDPRKFLKPAMD | acetylation | [1] | 345 | AEMAKRYKSGALDPQ | acetylation | [1] |
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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 | REGION 233 235 Dihydroxyacetone phosphate binding (By REGION 275 278 Dihydroxyacetone phosphate binding (By ACT_SITE 83 83 Proton donor (By similarity). BINDING 199 199 Dihydroxyacetone phosphate; via amide |
Keyword | Complete proteome; Lyase; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 361 AA |
Protein Sequence | MARITLRQLL DHAAEHGYGV PAFNINNMEQ GLAIMEAAAL VDAPVIIQAS RGARSYANDI 60 MLAKMIDALA EMYPDIPLCM HQDHGNDEAT CATAIRYGFT SVMMDGSLKA DAKTAADYQY 120 NVDITRRVVD MAHWVGASVE GELGVLGSLE HGGGEQEDGH GVEGKVSREQ LLTDPDQAVE 180 FVRATKVDAL AIAMGTSHGA YKFSRKPDGD VLAMKVVEEI HRRLPNTHLV MHGSSSVPQD 240 LQDIFNEFGG AMPQTFGVPV EEIVRGIKHG VRKVNIDTDC RLAMTGVFRK VATQNKAEFD 300 PRKFLKPAMD AMRDICKLRF EQFGTAGNAS KIKVVPMAEM AKRYKSGALD PQIGQVARAA 360 E 361 |
Gene Ontology | GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:InterPro. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006096; P:glycolysis; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |