Hmdb loader
Survey
You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.

Showing Protein Serine hydroxymethyltransferase, mitochondrial (HMDBP00792)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 8 metabolites
Identification
HMDB Protein ID HMDBP00792
Secondary Accession Numbers
  • 6072
  • HMDBP03595
  • HMDBP09001
Name Serine hydroxymethyltransferase, mitochondrial
Synonyms
  1. Glycine hydroxymethyltransferase
  2. SHMT
  3. Serine methylase
Gene Name SHMT2
Protein Type Enzyme
Biological Properties
General Function Involved in catalytic activity
Specific Function Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Interconversion of serine and glycine. Associates with mitochondrial DNA.
Pathways
  • 3-Phosphoglycerate dehydrogenase deficiency
  • Cyanoamino acid metabolism
  • Dihydropyrimidine Dehydrogenase Deficiency (DHPD)
  • Dimethylglycine Dehydrogenase Deficiency
  • Dimethylglycine Dehydrogenase Deficiency
  • Glycine, serine and threonine metabolism
  • Glycine, serine and threonine metabolism
  • Glyoxylate and dicarboxylate metabolism
  • Hyperglycinemia, non-ketotic
  • Non Ketotic Hyperglycinemia
  • One carbon pool by folate
  • Sarcosine Oncometabolite Pathway
  • Sarcosinemia
  • tetrahydrofolate interconversion
Reactions
5,10-Methylene-THF + Glycine + Water → Tetrahydrofolic acid + L-Serine details
L-Serine + 5,6,7,8-Tetrahydromethanopterin → 5,10-Methylenetetrahydromethanopterin + Glycine + Water details
GO Classification
Biological Process
positive regulation of cell proliferation
tetrahydrofolate interconversion
protein homotetramerization
glycine biosynthetic process from serine
L-serine biosynthetic process
one-carbon metabolic process
Cellular Component
microtubule cytoskeleton
mitochondrial nucleoid
mitochondrial inner membrane
mitochondrial intermembrane space
Function
binding
catalytic activity
transferase activity
glycine hydroxymethyltransferase activity
cofactor binding
pyridoxal phosphate binding
transferase activity, transferring one-carbon groups
methyltransferase activity
Molecular Function
pyridoxal phosphate binding
chromatin binding
glycine hydroxymethyltransferase activity
L-allo-threonine aldolase activity
methyltransferase activity
amino acid binding
Process
metabolic process
cellular metabolic process
serine family amino acid metabolic process
glycine metabolic process
l-serine metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
Cellular Location
  1. Mitochondrion
Gene Properties
Chromosome Location 12
Locus 12q12-q14
SNPs SHMT2
Gene Sequence 
>1515 bp
ATGCTGTACTTCTCTTTGTTTTGGGCGGCTCGGCCTCTGCAGAGATGTGGGCAGCTGGTC
AGGATGGCCATTCGGGCTCAGCACAGCAACGCAGCCCAGACTCAGACTGGGGAAGCAAAC
AGGGGCTGGACAGGCCAGGAGAGCCTGTCGGACAGTGATCCTGAGATGTGGGAGTTGCTG
CAGAGGGAGAAGGACAGGCAGTGTCGTGGCCTGGAGCTCATTGCCTCAGAGAACTTCTGC
AGCCGAGCTGCGCTGGAGGCCCTGGGGTCCTGTCTGAACAACAAGTACTCGGAGGGTTAT
CCTGGCAAGAGATACTATGGGGGAGCAGAGGTGGTGGATGAAATTGAGCTGCTGTGCCAG
CGCCGGGCCTTGGAAGCCTTTGACCTGGATCCTGCACAGTGGGGAGTCAATGTCCAGCCC
TACTCCGGGTCCCCAGCCAACCTGGCCGTCTACACAGCCCTTCTGCAACCTCACGACCGG
ATCATGGGGCTGGACCTGCCCGATGGGGGCCATCTCACCCACGGCTACATGTCTGACGTC
AAGCGGATATCAGCCACGTCCATCTTCTTCGAGTCTATGCCCTATAAGCTCAACCCCAAA
ACTGGCCTCATTGACTACAACCAGCTGGCACTGACTGCTCGACTTTTCCGGCCACGGCTC
ATCATAGCTGGCACCAGCGCCTATGCTCGCCTCATTGACTACGCCCGCATGAGAGAGGTG
TGTGATGAAGTCAAAGCACACCTGCTGGCAGACATGGCCCACATCAGTGGCCTGGTGGCT
GCCAAGGTGATTCCCTCGCCTTTCAAGCACGCGGACATCGTCACCACCACTACTCACAAG
ACTCTTCGAGGGGCCAGGTCAGGGCTCATCTTCTACCGGAAAGGGGTGAAGGCTGTGGAC
CCCAAGACTGGCCGGGAGATCCCTTACACATTTGAGGACCGAATCAACTTTGCCGTGTTC
CCATCCCTGCAGGGGGGCCCCCACAATCATGCCATTGCTGCAGTAGCTGTGGCCCTAAAG
CAGGCCTGCACCCCCATGTTCCGGGAGTACTCCCTGCAGGTTCTGAAGAATGCTCGGGCC
ATGGCAGATGCCCTGCTAGAGCGAGGCTACTCACTGGTATCAGGTGGTACTGACAACCAC
CTGGTGCTGGTGGACCTGCGGCCCAAGGGCCTGGATGGAGCTCGGGCTGAGCGGGTGCTA
GAGCTTGTATCCATCACTGCCAACAAGAACACCTGTCCTGGAGACCGAAGTGCCATCACA
CCGGGCGGCCTGCGGCTTGGGGCCCCAGCCTTAACTTCTCGACAGTTCCGTGAGGATGAC
TTCCGGAGAGTTGTGGACTTTATAGATGAAGGGGTCAACATTGGCTTAGAGGTGAAGAGC
AAGACTGCCAAGCTCCAGGATTTCAAATCCTTCCTGCTTAAGGACTCAGAAACAAGTCAG
CGTCTGGCCAACCTCAGGCAACGGGTGGAGCAGTTTGCCAGGGCCTTCCCCATGCCTGGT
TTTGATGAGCATTGA
Protein Properties
Number of Residues 504
Molecular Weight 54862.125
Theoretical pI 8.531
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence 
>Serine hydroxymethyltransferase, mitochondrial
MLYFSLFWAARPLQRCGQLVRMAIRAQHSNAAQTQTGEANRGWTGQESLSDSDPEMWELL
QREKDRQCRGLELIASENFCSRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQ
RRALEAFDLDPAQWGVNVQPYSGSPANLAVYTALLQPHDRIMGLDLPDGGHLTHGYMSDV
KRISATSIFFESMPYKLNPKTGLIDYNQLALTARLFRPRLIIAGTSAYARLIDYARMREV
CDEVKAHLLADMAHISGLVAAKVIPSPFKHADIVTTTTHKTLRGARSGLIFYRKGVKAVD
PKTGREIPYTFEDRINFAVFPSLQGGPHNHAIAAVAVALKQACTPMFREYSLQVLKNARA
MADALLERGYSLVSGGTDNHLVLVDLRPKGLDGARAERVLELVSITANKNTCPGDRSAIT
PGGLRLGAPALTSRQFREDDFRRVVDFIDEGVNIGLEVKSKTAKLQDFKSFLLKDSETSQ
RLANLRQRVEQFARAFPMPGFDEH
GenBank ID Protein 15080303
UniProtKB/Swiss-Prot ID P34897
UniProtKB/Swiss-Prot Entry Name GLYM_HUMAN
PDB IDs
GenBank Gene ID BC011911
GeneCard ID SHMT2
GenAtlas ID SHMT2
HGNC ID HGNC:10852
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Stover PJ, Chen LH, Suh JR, Stover DM, Keyomarsi K, Shane B: Molecular cloning, characterization, and regulation of the human mitochondrial serine hydroxymethyltransferase gene. J Biol Chem. 1997 Jan 17;272(3):1842-8. [PubMed:8999870 ]
  4. Garrow TA, Brenner AA, Whitehead VM, Chen XN, Duncan RG, Korenberg JR, Shane B: Cloning of human cDNAs encoding mitochondrial and cytosolic serine hydroxymethyltransferases and chromosomal localization. J Biol Chem. 1993 Jun 5;268(16):11910-6. [PubMed:8505317 ]
  5. Snell K, Baumann U, Byrne PC, Chave KJ, Renwick SB, Sanders PG, Whitehouse SK: The genetic organization and protein crystallographic structure of human serine hydroxymethyltransferase. Adv Enzyme Regul. 2000;40:353-403. [PubMed:10828359 ]