ID GLYA_NEIG1 Reviewed; 416 AA. AC Q5F8C0; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 1. DT 05-MAY-2009, entry version 30. DE RecName: Full=Serine hydroxymethyltransferase; DE Short=Serine methylase; DE Short=SHMT; DE EC=2.1.2.1; GN Name=glyA; OrderedLocusNames=NGO0866; OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=242231; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=99348393; PubMed=10417653; RX DOI=10.1046/j.1365-2958.1999.01514.x; RA Zhu P., Morelli G., Achtman M.; RT "The opcA and (psi)opcB regions in Neisseria: genes, pseudogenes, RT deletions, insertion elements and DNA islands."; RL Mol. Microbiol. 33:635-650(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S., RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.; RT "The complete genome sequence of Neisseria gonorrhoeae."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Interconversion of serine and glycine. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine + CC H(2)O = tetrahydrofolate + L-serine. CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate pathway. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the SHMT family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ242839; CAB45001.1; -; Genomic_DNA. DR EMBL; AE004969; AAW89567.1; -; Genomic_DNA. DR RefSeq; YP_207979.1; -. DR GeneID; 3281886; -. DR GenomeReviews; AE004969_GR; NGO0866. DR KEGG; ngo:NGO0866; -. DR NMPDR; fig|242231.4.peg.232; -. DR HOGENOM; Q5F8C0; -. DR OMA; Q5F8C0; TNASTES. DR BioCyc; NGON242231:NGO0866-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:HAMAP. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0006544; P:glycine metabolic process; IEA:InterPro. DR GO; GO:0006563; P:L-serine metabolic process; IEA:InterPro. DR GO; GO:0006730; P:one-carbon compound metabolic process; IEA:HAMAP. DR HAMAP; MF_00051; -; 1. DR InterPro; IPR001085; Gly_HO-MeTrfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1. DR PANTHER; PTHR11680; Gly_HO-Metrfase; 1. DR Pfam; PF00464; SHMT; 1. DR PIRSF; PIRSF000412; SHMT; 1. DR PROSITE; PS00096; SHMT; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; One-carbon metabolism; KW Pyridoxal phosphate; Transferase. FT CHAIN 1 416 Serine hydroxymethyltransferase. FT /FTId=PRO_0000113620. FT BINDING 229 229 Pyridoxal phosphate (covalent) (By FT similarity). SQ SEQUENCE 416 AA; 44990 MW; F53A0C9274D00219 CRC64; MFSKSVTLAQ YDPDLAAAIA QEDRRQQDHV ELIASENYVS CAVMEAQGSQ LTNKYAEGYP AKRYYGGCEY VDIVEQLAID RVKELFGAAY ANVQPHSGSQ ANQAVYASVL KPGDTILGMS LAHGGHLTHG ASVNISGKLY NAVTYGLDEN EVLDYAEVER LALEHKPKMI VAGASAYALQ IDWAKFREIA DKVGAYLFVD MAHYAGLVAG GEYPNPVPFC DFVTTTTHKT LRGPRGGVIL CRDNTHEKAL NSSIFPSLQG GPLMHVIAAK AVAFKEALQP EFKQYAKQVK INAAVMAEEL VKRGLRIVSG RTESHVFLVD LQPMKITGKA AEAALGKAHI TVNKNAIPND PEKPFVTSGI RIGSAAMTTR GFNETDARVL SNLVADVLAN PEDEANLAKV RGQVTALCDK YPVYGT //