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Database: UniProt
Entry: Q4QTL5_WOLPI
LinkDB: Q4QTL5_WOLPI
Original site: Q4QTL5_WOLPI 
ID   Q4QTL5_WOLPI            Unreviewed;       320 AA.
AC   Q4QTL5;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Serine hydroxymethyltransferase {ECO:0000313|EMBL:AAY81978.1};
DE   Flags: Fragment;
GN   Name=glyA {ECO:0000313|EMBL:AAY81978.1};
OS   Wolbachia pipientis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=955 {ECO:0000313|EMBL:AAY81978.1};
RN   [1] {ECO:0000313|EMBL:AAY81978.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WRi {ECO:0000313|EMBL:AAY81978.1};
RX   PubMed=16269725; DOI=10.1128/AEM.71.11.6910-6917.2005;
RA   Mavingui P., Van V.T., Labeyrie E., Rances E., Vavre F., Simonet P.;
RT   "Efficient procedure for purification of obligate intracellular Wolbachia
RT   pipientis and representative amplification of its genome by multiple-
RT   displacement amplification.";
RL   Appl. Environ. Microbiol. 71:6910-6917(2005).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the SHMT family.
CC       {ECO:0000256|ARBA:ARBA00006376}.
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DR   EMBL; AY833067; AAY81978.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4QTL5; -.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
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:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:InterPro.
DR   CDD; cd00378; SHMT; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11680:SF28; SERINE HYDROXYMETHYLTRANSFERASE; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00096; SHMT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Methyltransferase {ECO:0000313|EMBL:AAY81978.1};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAY81978.1}.
FT   DOMAIN          1..320
FT                   /note="Serine hydroxymethyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00464"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAY81978.1"
FT   NON_TER         320
FT                   /evidence="ECO:0000313|EMBL:AAY81978.1"
SQ   SEQUENCE   320 AA;  34573 MW;  66FA812C2689AA32 CRC64;
     KAVMEAQGSF LTNKYAEGYP GKRYYCGCEH VDKIESLAIE RLCKLFGVKF ANVQPHSGSQ
     ANQAVFASLL TPGDTILGLS LSCGGHLTHG AAPSLSGKWF KSIQYTVNKD TYLLDMDEIE
     KLALEHKPKL IIAGASAYPR KMDFKRFREI ADKVGAYLLA DIAHYAGLIA AGEYPSPAEY
     AHVMTSTTHK TLRGPRGGIV MTNDEILHKK IQSAVFPGLQ GGPLMHVIAA KAVAFKEALA
     PGFKTYSKKV VENAKVLAQE LQKHGLDIIT GGTDSHIVLV DLRSQKLTGK DVVDSLERAG
     ITCNKNSVPF DTAKPTITSG
//
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