GLYC_CANAL
ID GLYC_CANAL Reviewed; 470 AA.
AC O13426; A0A1D8PQ92; Q5A8J8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 4.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Serine hydroxymethyltransferase, cytosolic;
DE Short=SHMT;
DE EC=2.1.2.1;
DE AltName: Full=Glycine hydroxymethyltransferase;
DE AltName: Full=SHMII;
DE AltName: Full=Serine methylase;
GN Name=SHM2; OrderedLocusNames=CAALFM_C603760CA;
GN ORFNames=CaO19.13173, CaO19.5750;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10641038;
RX DOI=10.1002/(sici)1097-0061(20000130)16:2<167::aid-yea519>3.0.co;2-1;
RA McNeil J.B., Flynn J., Tsao N., Monschau N., Stahmann K., Haynes R.H.,
RA McIntosh E.M., Pearlman R.E.;
RT "Glycine metabolism in Candida albicans: characterization of the serine
RT hydroxymethyltransferase (SHM1, SHM2) and threonine aldolase (GLY1)
RT genes.";
RL Yeast 16:167-175(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5]
RP PROTEIN SEQUENCE OF 2-11 AND 191-199, ACETYLATION AT SER-2, SUBCELLULAR
RP LOCATION, AND ANTIGENICITY.
RC STRAIN=SC5314 / ATCC MYA-2876; TISSUE=Protoplast;
RX PubMed=15378761; DOI=10.1002/pmic.200400903;
RA Pitarch A., Abian J., Carrascal M., Sanchez M., Nombela C., Gil C.;
RT "Proteomics-based identification of novel Candida albicans antigens for
RT diagnosis of systemic candidiasis in patients with underlying hematological
RT malignancies.";
RL Proteomics 4:3084-3106(2004).
CC -!- FUNCTION: Interconversion of serine and glycine.
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:0000269|PubMed:15378761}.
CC -!- MISCELLANEOUS: In eukaryotes there are two forms of the enzymes: a
CC cytosolic one and a mitochondrial one.
CC -!- MISCELLANEOUS: Has antigenic properties.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR EMBL; AF009966; AAB64197.1; -; Genomic_DNA.
DR EMBL; CP017628; AOW30303.1; -; Genomic_DNA.
DR RefSeq; XP_718086.1; XM_712993.1.
DR AlphaFoldDB; O13426; -.
DR SMR; O13426; -.
DR STRING; 237561.O13426; -.
DR iPTMnet; O13426; -.
DR COMPLUYEAST-2DPAGE; O13426; -.
DR PRIDE; O13426; -.
DR GeneID; 3640306; -.
DR KEGG; cal:CAALFM_C603760CA; -.
DR CGD; CAL0000189123; SHM2.
DR VEuPathDB; FungiDB:C6_03760C_A; -.
DR eggNOG; KOG2467; Eukaryota.
DR HOGENOM; CLU_022477_0_1_1; -.
DR InParanoid; O13426; -.
DR OMA; SHPAGLI; -.
DR OrthoDB; 372408at2759; -.
DR UniPathway; UPA00193; -.
DR PRO; PR:O13426; -.
DR Proteomes; UP000000559; Chromosome 6.
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 PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; One-carbon metabolism;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15378761"
FT CHAIN 2..470
FT /note="Serine hydroxymethyltransferase, cytosolic"
FT /id="PRO_0000113511"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:15378761"
FT MOD_RES 249
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 82
FT /note="D -> H (in Ref. 1; AAB64197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 52038 MW; 8FC84DF98EBD12D0 CRC64;
MSAYALSQSH RQLTEGHLKD TDPEVDQIIK DEIDRQQHSI VLIASENFTT TAVFDALGTP
MCNKYSEGYP GARYYGGNEH IDRMELLCQE RALKAFGLTP DKWGVNVQTL SGSPANLQVY
QAIMKPHERL MGLDLPHGGH LSHGYQTDSR KISAVSTYFE TMPYRVDLET GLIDYDMLEK
TAVLYRPKVL VAGTSAYCRL IDYKRMREIA DKVGAYLVVD MAHISGLIAA GVIPSPFEYA
DIVTTTTHKS LRGPRGAMIF FRRGVRSVNP KTGQEILYDL ENPINFSVFP GHQGGPHNHT
IAALATALKQ ANTPEFKEYQ EQVLKNAKAL ESEFTKKGYK LVSDGTDSHM VLVSLKDKQI
DGARVETVCE KINIALNKNS IPGDKSALVP GGVRIGAPAM TTRGLGEEDF KKIVSYIDFA
VNYAKEVQSQ LPKDANKLKD FKNAVSGDSE KLKAVRDEIY QWAGSFPLAV
