ID I4CEU0_DESTA Unreviewed; 533 AA.
AC I4CEU0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=B12 binding domain/Pterin binding enzyme {ECO:0000313|EMBL:AFM28081.1};
GN OrderedLocusNames=Desti_5499 {ECO:0000313|EMBL:AFM28081.1};
OS Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1).
OC Bacteria; Thermodesulfobacteriota; Desulfomonilia; Desulfomonilales;
OC Desulfomonilaceae; Desulfomonile.
OX NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM28081.1, ECO:0000313|Proteomes:UP000006055};
RN [1] {ECO:0000313|Proteomes:UP000006055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49306 / DSM 6799 / DCB-1
RC {ECO:0000313|Proteomes:UP000006055};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Zeytun A.,
RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the vitamin-B12 dependent methionine synthase
CC family. {ECO:0000256|ARBA:ARBA00010398}.
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DR EMBL; CP003360; AFM28081.1; -; Genomic_DNA.
DR AlphaFoldDB; I4CEU0; -.
DR STRING; 706587.Desti_5499; -.
DR KEGG; dti:Desti_5499; -.
DR PATRIC; fig|706587.4.peg.6193; -.
DR eggNOG; COG1410; Bacteria.
DR HOGENOM; CLU_510684_0_0_7; -.
DR OrthoDB; 9803687at2; -.
DR Proteomes; UP000006055; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR Gene3D; 1.10.1240.10; Methionine synthase domain; 1.
DR InterPro; IPR003759; Cbl-bd_cap.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR011005; Dihydropteroate_synth-like_sf.
DR InterPro; IPR036594; Meth_synthase_dom.
DR InterPro; IPR000489; Pterin-binding_dom.
DR PANTHER; PTHR45833; METHIONINE SYNTHASE; 1.
DR PANTHER; PTHR45833:SF1; METHIONINE SYNTHASE; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF02607; B12-binding_2; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SMART; SM01018; B12-binding_2; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR SUPFAM; SSF47644; Methionine synthase domain; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
DR PROSITE; PS51337; B12_BINDING_NTER; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000006055};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..245
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
FT DOMAIN 313..406
FT /note="B12-binding N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51337"
FT DOMAIN 408..533
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 533 AA; 57621 MW; EB6417A8615C7BC3 CRC64;
MIIIGEKING TRKAVAAAIK KRDSSFIQDL ALSQVRGGAH FLDVNAGTHP DSEPDDITWL
VNTVQEVTDT NLCIDSANPK ALLAGITAAK KLPMINSLSG EKARIQGVLP LASQYGTDLV
VLALDDNGIP KTAEDRLEIV RRLVGLCVEN GLTEAQLYVD PLVTTIATDN QSGIVAFETI
RRIKQEFPNI HLTCGLSNIS FGQPSRGIIN QAFAALAIGA GLDSAIVDPN DRELRNIIYS
AEMVLGQDPD CMNFNQAFRE GHIGSSKGVS GSYKETISRA LQGLITTLQQ AGVIDSTIIS
ASDQEKQASK AETVAEESEG NVLEDIVESL VGMKKDRVKT LTEQALSSGT DPMLILDASR
RAMTEVGRLF ETEEYFVPEL ILAGRMLKEI SDAVKPYLSD GTSEGPKKGR VIIGTVAGDI
HDIGKDIVVT MLDINGYEVL DLGVDVPNER FVEAARDFKP DVIGLSGFLT LAYDPMKDTI
AAIREENIRE IKFMIGGGQI DDHIREYTQA DAYGNDAMDA VRLCEQWING AGK
//
