ID A0A1G2QNH5_9BACT Unreviewed; 299 AA.
AC A0A1G2QNH5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Serine hydroxymethyltransferase {ECO:0000313|EMBL:OHA62184.1};
DE Flags: Fragment;
GN Name=glyA {ECO:0000313|EMBL:OHA62184.1};
GN ORFNames=A2556_00975 {ECO:0000313|EMBL:OHA62184.1};
OS Candidatus Vogelbacteria bacterium RIFOXYD2_FULL_44_9.
OC Bacteria; Candidatus Vogelbacteria.
OX NCBI_TaxID=1802441 {ECO:0000313|EMBL:OHA62184.1, ECO:0000313|Proteomes:UP000177140};
RN [1] {ECO:0000313|EMBL:OHA62184.1, ECO:0000313|Proteomes:UP000177140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OHA62184.1}.
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DR EMBL; MHTM01000019; OHA62184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2QNH5; -.
DR Proteomes; UP000177140; Unassembled WGS sequence.
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 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:OHA62184.1};
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OHA62184.1}.
FT DOMAIN 6..298
FT /note="Serine hydroxymethyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF00464"
FT NON_TER 299
FT /evidence="ECO:0000313|EMBL:OHA62184.1"
SQ SEQUENCE 299 AA; 32956 MW; D10657DB996993F5 CRC64;
MLALMDMVDQ QIEKLIKAEA NKQKKTINLI ASENYVSADV RKALGSEFVN KYAEGYPGKR
YYGGNQFSDE LESLCQKRAL KAFSLSAKKW AVNVQPLSGS PANLAVYLAL VPFGEKIMGM
TLSSGGHLSH GHKVSWTGKA WEQVTYGVDE KTERLDYEQL MQLAKKNKPQ IIVAGFTAYP
RKIDWKKFRE IADAVGAHLM VDMSHLAGLV AGGVYPSPFP YADIVTTTTH KTLRGPRSAL
IFSKIDERNL PAKIDKAVFP GIQGGPHLNQ IASVAVALAE ATRPEFKQYA KQIVKNAQT
//
