GLYC7_ARATH
ID GLYC7_ARATH Reviewed; 598 AA.
AC Q84WV0; Q8LFB5; Q9C8X6;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Serine hydroxymethyltransferase 7;
DE Short=AtSHMT7;
DE EC=2.1.2.1;
DE AltName: Full=Glycine hydroxymethyltransferase 7;
DE AltName: Full=Serine methylase 7;
GN Name=SHM7; Synonyms=SHMT7; OrderedLocusNames=At1g36370; ORFNames=F7F23.9;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52195.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM61506.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC021199; AAG52195.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE31862.1; -; Genomic_DNA.
DR EMBL; BT002738; AAO22567.1; -; mRNA.
DR EMBL; AY084945; AAM61506.1; ALT_INIT; mRNA.
DR PIR; F86484; F86484.
DR RefSeq; NP_564473.1; NM_103323.3.
DR AlphaFoldDB; Q84WV0; -.
DR SMR; Q84WV0; -.
DR STRING; 3702.AT1G36370.1; -.
DR iPTMnet; Q84WV0; -.
DR PaxDb; Q84WV0; -.
DR PRIDE; Q84WV0; -.
DR ProteomicsDB; 248529; -.
DR EnsemblPlants; AT1G36370.1; AT1G36370.1; AT1G36370.
DR GeneID; 840543; -.
DR Gramene; AT1G36370.1; AT1G36370.1; AT1G36370.
DR KEGG; ath:AT1G36370; -.
DR Araport; AT1G36370; -.
DR TAIR; locus:2035937; AT1G36370.
DR eggNOG; KOG2467; Eukaryota.
DR HOGENOM; CLU_022477_0_1_1; -.
DR InParanoid; Q84WV0; -.
DR OMA; VVENDQY; -.
DR OrthoDB; 372408at2759; -.
DR PhylomeDB; Q84WV0; -.
DR BioCyc; ARA:AT1G36370-MON; -.
DR UniPathway; UPA00193; -.
DR PRO; PR:Q84WV0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84WV0; baseline and differential.
DR Genevisible; Q84WV0; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0044030; P:regulation of DNA methylation; IMP:TAIR.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IMP:TAIR.
DR GO; GO:0055063; P:sulfate ion homeostasis; IMP:TAIR.
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..598
FT /note="Serine hydroxymethyltransferase 7"
FT /id="PRO_0000422352"
FT REGION 57..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 370
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 299
FT /note="L -> V (in Ref. 4; AAM61506)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 598 AA; 66294 MW; 07AA294C41E1FD85 CRC64;
MDLSRSQTNF QLGFGCSHAS MTPTPTPRAP IADDSINLQV DQSFRSLPTT FSPIPLQLLE
QKAEKTTTVD EPKKDGGGGG DQKEDEHFRI LGHHMCLKRQ RDCPLLLTQS KHPKRSSIGD
SDLESRRAAV RAWGDQPIHL ADPDIHELME KEKQRQVRGI ELIASENFVC RAVMEALGSH
LTNKYSEGMP GARYYTGNQY IDQIENLCIE RALTAFGLES DKWGVNVQPY SCTSANFAVY
TGLLLPGERI MGLDSPSGGH MSHGYCTPGG KKISAASIFF ESFPYKVNPQ TGYIDYDKLE
DKALDYRPKI LICGGSSYPR DWDFARVRQI ADKCGAVLMC DMAHISGLVA TKECSNPFDH
CDIVTSTTHK GLRGPRGGII FYRRGPKIRK QGHHSSHCDT STHYDLEEKI NFAVFPSLQG
GPHNNHIAAL AIALKQVATP EYKAYIQQMK KNAQALAAAL LRRKCRLVTG GTDNHLLLWD
LTPMGLTGKV YEKVCEMCHI TLNKTAIFGD NGTISPGGVR IGTPAMTTRG CIESDFETMA
DFLIKAAQIT SALQREHGKS HKEFVKSLCT NKDIAELRNR VEAFALQYEM PASLIRIE
