GLYC6_ARATH
ID GLYC6_ARATH Reviewed; 599 AA.
AC Q9LM59;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Serine hydroxymethyltransferase 6;
DE Short=AtSHMT6;
DE EC=2.1.2.1;
DE AltName: Full=Glycine hydroxymethyltransferase 6;
DE AltName: Full=Serine methylase 6;
GN Name=SHM6; Synonyms=SHMT6; OrderedLocusNames=At1g22020; ORFNames=F2E2.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP REVIEW.
RX PubMed=12730263; DOI=10.1093/jxb/erg171;
RA Bauwe H., Kolukisaoglu U.;
RT "Genetic manipulation of glycine decarboxylation.";
RL J. Exp. Bot. 54:1523-1535(2003).
RN [5]
RP GENE FAMILY.
RX PubMed=20518745; DOI=10.1042/bj20100566;
RA Zhang Y., Sun K., Sandoval F.J., Santiago K., Roje S.;
RT "One-carbon metabolism in plants: characterization of a plastid serine
RT hydroxymethyltransferase.";
RL Biochem. J. 430:97-105(2010).
CC -!- FUNCTION: Catalyzes the interconversion of serine and glycine.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR EMBL; AC069252; AAF86546.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30186.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60843.1; -; Genomic_DNA.
DR EMBL; AY125514; AAM78106.1; -; mRNA.
DR EMBL; BT004532; AAO42778.1; -; mRNA.
DR RefSeq; NP_001323098.1; NM_001332533.1.
DR RefSeq; NP_173621.1; NM_102052.3.
DR AlphaFoldDB; Q9LM59; -.
DR SMR; Q9LM59; -.
DR STRING; 3702.AT1G22020.1; -.
DR PaxDb; Q9LM59; -.
DR PRIDE; Q9LM59; -.
DR ProteomicsDB; 248528; -.
DR EnsemblPlants; AT1G22020.1; AT1G22020.1; AT1G22020.
DR EnsemblPlants; AT1G22020.2; AT1G22020.2; AT1G22020.
DR GeneID; 838807; -.
DR Gramene; AT1G22020.1; AT1G22020.1; AT1G22020.
DR Gramene; AT1G22020.2; AT1G22020.2; AT1G22020.
DR KEGG; ath:AT1G22020; -.
DR Araport; AT1G22020; -.
DR TAIR; locus:2030581; AT1G22020.
DR eggNOG; KOG2467; Eukaryota.
DR HOGENOM; CLU_022477_0_1_1; -.
DR InParanoid; Q9LM59; -.
DR OMA; SIQREHG; -.
DR OrthoDB; 372408at2759; -.
DR PhylomeDB; Q9LM59; -.
DR BioCyc; ARA:AT1G22020-MON; -.
DR UniPathway; UPA00193; -.
DR PRO; PR:Q9LM59; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LM59; baseline and differential.
DR Genevisible; Q9LM59; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0070905; F:serine binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0046655; P:folic acid metabolic process; IBA:GO_Central.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IBA:GO_Central.
DR GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IBA:GO_Central.
DR CDD; cd00378; SHMT; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00051; SHMT; 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR001085; Ser_HO-MeTrfase.
DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR InterPro; IPR039429; SHMT-like_dom.
DR PANTHER; PTHR11680; PTHR11680; 1.
DR Pfam; PF00464; SHMT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; One-carbon metabolism; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..599
FT /note="Serine hydroxymethyltransferase 6"
FT /id="PRO_0000422351"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 374
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 599 AA; 66647 MW; 94A0B57857CDBE57 CRC64;
MDRIAQSDLS LGFGSSHALP LPHPPRIPIA DDSITLQIDS SFRPSSNPMP PVPLQLLEQR
FDVTGSCSRV VEEDDEVVGD NDDDDQREEE QFILLGHPMK LKRGRGGNSY SLASSSPCKR
FVVDSGIESR RAVVRAWGNQ SIEEADPEIH EFMEKEKQRQ FRGIELIASE NFVCRAVMEA
LGSHLTNKYS EGMPGARYYT GNQYIDQIEI LCQERALAAF GLNHEKWGVN VQPYSCTSAN
FAVFTGLLMP GERIMGLDSP SGGHMSHGYY TPGGKKVSGA SIFFESFPYK VDPRTGYIDY
DKLEEKALDY RPKILICGGS SYPRDWEFPR FRHIADKCGA VLMFDMAQIS GLVAAKESPN
PFDYCDIVTS TTHKSLRGPR GGIIFYKRGL KPKKQSINLN HCESNIQYDF EEKINFSVFP
SLQGGPHNNH IAALAIALKQ AASPEYKLYM RQVKKNAKAL ASALISRKCK LITGGTDNHL
LLWDLTPLGL TGKVYEKVCE MCHITVNKVA IFSENGVISP GGVRIGSPAM TSRGCLEPEF
ETMADFLYRA AQIASAAQRE HGKLQKEPLK SIYHCKEIAD LRNQVEAFAT QFAMPAFDM
