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LOCUS WP_000919165 417 aa linear BCT 10-FEB-2020 ACCESSION WP_000919165 VERSION WP_000919165.1 KEYWORDS RefSeq. SOURCE Escherichia coli ORGANISM Escherichia coli Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. REFERENCE 1 (residues 1 to 417) AUTHORS Vivoli,M., Angelucci,F., Ilari,A., Morea,V., Angelaccio,S., di Salvo,M.L. and Contestabile,R. TITLE Role of a conserved active site cation-pi interaction in Escherichia coli serine hydroxymethyltransferase JOURNAL Biochemistry 48 (50), 12034-12046 (2009) PUBMED 19883126 REFERENCE 2 (residues 1 to 417) AUTHORS Bhatt,A.N. and Bhakuni,V. TITLE Characterization of pyridoxal 5'- phosphate-binding domain and folding intermediate of Bacillus subtilis serine hydroxymethyltransferase: an autonomous folding domain JOURNAL J. Biochem. 144 (3), 295-303 (2008) PUBMED 18483062 REFERENCE 3 (residues 1 to 417) AUTHORS Fu,T.F., Boja,E.S., Safo,M.K. and Schirch,V. TITLE Role of proline residues in the folding of serine hydroxymethyltransferase JOURNAL J. Biol. Chem. 278 (33), 31088-31094 (2003) PUBMED 12773539 REFERENCE 4 (residues 1 to 417) AUTHORS Bhatt,A.N., Prakash,K., Subramanya,H.S. and Bhakuni,V. TITLE Different unfolding pathways for mesophilic and thermophilic homologues of serine hydroxymethyltransferase JOURNAL Biochemistry 41 (40), 12115-12123 (2002) PUBMED 12356312 REFERENCE 5 (residues 1 to 417) AUTHORS Contestabile,R., Angelaccio,S., Bossa,F., Wright,H.T., Scarsdale,N., Kazanina,G. and Schirch,V. TITLE Role of tyrosine 65 in the mechanism of serine hydroxymethyltransferase JOURNAL Biochemistry 39 (25), 7492-7500 (2000) PUBMED 10858298 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: BlastRule Evidence Accession :: NBR006908 Evidence Source :: NCBI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..417 /organism="Escherichia coli" /db_xref="taxon:562" gene 1..417 /gene="glyA" Protein 1..417 /product="serine hydroxymethyltransferase" /EC_number="2.1.2.1" /calculated_mol_wt=45214 Region 6..417 /region_name="glyA" /note="serine hydroxymethyltransferase; Reviewed; PRK00011" /db_xref="CDD:234571" Site order(12,14,21..22,31,36,54,72..73,81,96,103,138..139,265, 283) /site_type="other" /note="dimer interface [polypeptide binding]" /db_xref="CDD:99733" Site order(35,55,65,98..99,126,175,200,203,228..229,235,363) /site_type="other" /note="glycine-pyridoxal phosphate binding site [chemical binding]" /db_xref="CDD:99733" Site order(35,126,229,363) /site_type="active" /db_xref="CDD:99733" Site order(57,64,121,125,127,257,347) /site_type="other" /note="folate binding site [chemical binding]" /db_xref="CDD:99733" ORIGIN 1 mlkremniad ydaelwqame qekvrqeehi eliasenyts prvmqaqgsq ltnkyaegyp 61 gkryyggcey vdiveqlaid rakelfgady anvqphsgsq anfavytall epgdtvlgmn 121 lahgghlthg spvnfsgkly nivpygidat ghidyadlek qakehkpkmi iggfsaysgv 181 vdwakmreia dsigaylfvd mahvaglvaa gvypnpvpha hvvtttthkt lagprgglil 241 akggseelyk klnsavfpgg qggplmhvia gkavalkeam epefktyqqq vaknakamve 301 vflergykvv sggtdnhlfl vdlvdknltg keadaalgra nitvnknsvp ndpkspfvts 361 girvgtpait rrgfkeveak elagwmcdvl dsindeavie rikgkvldic arypvya