ID A0A1G1A5Z5_9BACT Unreviewed; 268 AA.
AC A0A1G1A5Z5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Pterin-binding domain-containing protein {ECO:0000259|PROSITE:PS50972};
GN ORFNames=A2498_09940 {ECO:0000313|EMBL:OGV65852.1};
OS Lentisphaerae bacterium RIFOXYC12_FULL_60_16.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798582 {ECO:0000313|EMBL:OGV65852.1, ECO:0000313|Proteomes:UP000178496};
RN [1] {ECO:0000313|EMBL:OGV65852.1, ECO:0000313|Proteomes:UP000178496}
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 -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00010398}.
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:OGV65852.1}.
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DR EMBL; MHBQ01000059; OGV65852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1A5Z5; -.
DR STRING; 1798582.A2498_09940; -.
DR Proteomes; UP000178496; Unassembled WGS sequence.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR000489; Pterin-binding_dom.
DR PANTHER; PTHR45833:SF2; BIFUNCTIONAL HOMOCYSTEINE S-METHYLTRANSFERASE_5,10-METHYLENETETRAHYDROFOLATE REDUCTASE; 1.
DR PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..250
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 268 AA; 28501 MW; 39B318B71A964046 CRC64;
MLVIGERING MFEAIGEAIK NKDPKPVREM AEKQLAGGAD ALDINVGTRV PKAERAAAMR
WLIEVTREVT DKPLSIDNPS LETVRVGLQA ATIKGRAIIN STTGQAEKLA AFMGLAHEFG
AGIVGLSIDE NGVAATIEGK LEIGMRTLAA ATDAGVSIED VYLDPIILPV NCDQKAPGIV
IETIRQFRLL SDPAPHVVIG LSNLSQGATE RSLINRVFLT MAIGAGLDAS IHDPLDTELT
NTMVTAEILL NKAIYSDSYL TAYLQGKA
//
