Tag | Content |
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CPLM ID | CPLM-004540 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Arabinose 5-phosphate isomerase GutQ |
Protein Synonyms/Alias | API; G-API; Phosphosugar aldol-ketol isomerase |
Gene Name | gutQ |
Gene Synonyms/Alias | srlQ; b2708; JW5431 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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52 | VVVSGIGKSGHIGKK | acetylation | [1] | 58 | GKSGHIGKKIAATLA | acetylation | [1] | 115 | IIPRLEDKSIALLAM | acetylation | [1] | 125 | ALLAMTGKPTSPLGL | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Catalyzes the reversible aldol-ketol isomerization between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P). It appears that the physiological function of G-API may be to synthesize the regulatory molecule A5P, which in turn participates in the induction of the gut operon through an unknown mechanism. It is also able of sustaining the biosynthetic pathway of 3-deoxy-D-manno-octulosonate (KDO), a unique 8-carbon sugar component of lipopolysaccharides (LPSs). |
Sequence Annotation | DOMAIN 34 177 SIS. DOMAIN 203 261 CBS 1. DOMAIN 269 321 CBS 2. NP_BIND 49 54 ATP (Potential). REGION 68 69 Substrate binding (By similarity). REGION 107 116 Substrate binding (By similarity). REGION 141 143 Substrate binding (By similarity). METAL 75 75 Zinc (By similarity). BINDING 75 75 Substrate (By similarity). BINDING 81 81 Substrate (By similarity). BINDING 215 215 Substrate (By similarity). BINDING 267 267 Substrate (By similarity). |
Keyword | ATP-binding; CBS domain; Complete proteome; Direct protein sequencing; Isomerase; Lipopolysaccharide biosynthesis; Metal-binding; Nucleotide-binding; Reference proteome; Repeat; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 321 AA |
Protein Sequence | MSEALLNAGR QTLMLELQEA SRLPERLGDD FVRAANIILH CEGKVVVSGI GKSGHIGKKI 60 AATLASTGTP AFFVHPAEAL HGDLGMIESR DVMLFISYSG GAKELDLIIP RLEDKSIALL 120 AMTGKPTSPL GLAAKAVLDI SVEREACPMH LAPTSSTVNT LMMGDALAMA VMQARGFNEE 180 DFARSHPAGA LGARLLNKVH HLMRRDDAIP QVALTASVMD AMLELSRTGL GLVAVCDAQQ 240 QVQGVFTDGD LRRWLVGGGA LTTPVNEAMT VGGTTLQSQS RAIDAKEILM KRKITAAPVV 300 DENGKLTGAI NLQDFYQAGI I 321 |
Gene Ontology | GO:0019146; F:arabinose-5-phosphate isomerase activity; IDA:EcoCyc. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0030246; F:carbohydrate binding; IEA:InterPro. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0042710; P:biofilm formation; IMP:EcoCyc. GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IMP:UniProtKB. |
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