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Database: UniProt
Entry: A0A3Q3GA90_KRYMA
LinkDB: A0A3Q3GA90_KRYMA
Original site: A0A3Q3GA90_KRYMA 
ID   A0A3Q3GA90_KRYMA        Unreviewed;       441 AA.
AC   A0A3Q3GA90;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Serine hydroxymethyltransferase {ECO:0000256|RuleBase:RU000585};
DE            EC=2.1.2.1 {ECO:0000256|RuleBase:RU000585};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000020942.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000020942.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Interconversion of serine and glycine.
CC       {ECO:0000256|RuleBase:RU000585}.
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         Evidence={ECO:0000256|RuleBase:RU000585};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR000412-50, ECO:0000256|RuleBase:RU000585};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777, ECO:0000256|RuleBase:RU000585}.
CC   -!- SIMILARITY: Belongs to the SHMT family.
CC       {ECO:0000256|RuleBase:RU000585}.
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DR   RefSeq; XP_017272030.1; XM_017416541.1.
DR   AlphaFoldDB; A0A3Q3GA90; -.
DR   Ensembl; ENSKMAT00000021216.1; ENSKMAP00000020942.1; ENSKMAG00000015534.1.
DR   GeneTree; ENSGT00390000002762; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:InterPro.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00378; SHMT; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR   InterPro; IPR039429; SHMT-like_dom.
DR   PANTHER; PTHR11680; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11680:SF35; SERINE HYDROXYMETHYLTRANSFERASE, CYTOSOLIC; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00096; SHMT; 1.
PE   3: Inferred from homology;
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW   ECO:0000256|RuleBase:RU000585};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000412-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Transferase {ECO:0000256|RuleBase:RU000585}.
FT   DOMAIN          26..309
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   MOD_RES         256
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000412-50"
SQ   SEQUENCE   441 AA;  48541 MW;  6434D6A71B903289 CRC64;
     MSLRNGHSVT KETWDSHNKM MLEPLAVNDS EVFSIIKKEK HRQTYGLELI ASENFASRAV
     LEALGSCMNN KYSEGYPGQR YYGGTEHIDE LERLCQQRAL EAFGLNAEKW GVNVQPYSGS
     PANFAVYTAV VEPHGRIMGL DLPDGGHLTH GFMTEKKKIS ATSIFFESMP YKVNPETGYI
     DYDRLQENAR LFHPKLIIAG TSCYSRNLDY ARLKQIAAEN GAYLMGDMAH ISGLVAAGVV
     PSPFEHCDIV STTTHKTLRG CRAGVIFYRK GVRSVDAKGK ETLYNLESLI NQAVFPGLQG
     GPHNHAIAGG SDNHLILLDL RNKGTDGGRA EKVLEACAIA CNKNTCPGDK SALRPSGLRF
     GSPALTSRGL VEEDFKKVAH FIHRGIELTL EVQRSLDPKA TLKEFIQALA QGEKFQQQVA
     EIRAEVEAFA GQFPMPGLPE L
//
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