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Database: UniProt
Entry: R6VQ37_9FIRM
LinkDB: R6VQ37_9FIRM
Original site: R6VQ37_9FIRM 
ID   R6VQ37_9FIRM            Unreviewed;       272 AA.
AC   R6VQ37;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Pterin binding enzyme {ECO:0000313|EMBL:CDC94276.1};
GN   ORFNames=BN546_00022 {ECO:0000313|EMBL:CDC94276.1};
OS   Firmicutes bacterium CAG:227.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263010 {ECO:0000313|EMBL:CDC94276.1, ECO:0000313|Proteomes:UP000018294};
RN   [1] {ECO:0000313|EMBL:CDC94276.1, ECO:0000313|Proteomes:UP000018294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:227 {ECO:0000313|Proteomes:UP000018294};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CDC94276.1}.
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DR   EMBL; CBGC010000243; CDC94276.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6VQ37; -.
DR   STRING; 1263010.BN546_00022; -.
DR   Proteomes; UP000018294; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000018294};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..248
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
SQ   SEQUENCE   272 AA;  30056 MW;  66A84729CC430704 CRC64;
     MIIIGEKING SIPSVAKAIA ERDSEFIKER ARKQAAANAT YIDCCASVPE AEEVETLKWM
     IDCIQEVTDL PISVDSPSAD VLTQAYKFCK RPGIFNSVSG EGDKIDKIFP LMAQEENKDW
     QVIALLSDDT GIPKCAADRL RVFDKIMAKA KEYNINPSRI HIDPLVEMLC TSEDGIAMNI
     EVIQTVRKQY PSIHITAAVS NISFNLPVRK LINYGFLILA MNAGLDSAIM DPTNRDMLGL
     TYATEALLGE DEFCMEYIGA YREGLIGPLP KA
//
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