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Database: UniProt
Entry: B6AK93_9BACT
LinkDB: B6AK93_9BACT
Original site: B6AK93_9BACT 
ID   B6AK93_9BACT            Unreviewed;       334 AA.
AC   B6AK93;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Putative aminomethyltransferase {ECO:0000313|EMBL:EDZ40077.1};
GN   ORFNames=CGL2_11111099 {ECO:0000313|EMBL:EDZ40077.1};
OS   Leptospirillum sp. Group II '5-way CG'.
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=419541 {ECO:0000313|EMBL:EDZ40077.1};
RN   [1] {ECO:0000313|EMBL:EDZ40077.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14961025; DOI=10.1038/nature02340;
RA   Tyson G.W., Chapman J., Hugenholtz P., Allen E.E., Ram R.J.,
RA   Richardson P.M., Solovyev V.V., Rubin E.M., Rokhsar D.S., Banfield J.F.;
RT   "Community structure and metabolism through reconstruction of microbial
RT   genomes from the environment.";
RL   Nature 428:37-43(2004).
RN   [2] {ECO:0000313|EMBL:EDZ40077.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18651792; DOI=10.1371/journal.pbio.0060177;
RA   Simmons S.L., Dibartolo G., Denef V.J., Goltsman D.S., Thelen M.P.,
RA   Banfield J.F.;
RT   "Population genomic analysis of strain variation in Leptospirillum group II
RT   bacteria involved in acid mine drainage formation.";
RL   PLoS Biol. 6:E177-E177(2008).
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DR   EMBL; DS995259; EDZ40077.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6AK93; -.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   InterPro; IPR045179; YgfZ/GcvT.
DR   InterPro; IPR017703; YgfZ/GcvT_CS.
DR   NCBIfam; TIGR03317; ygfZ_signature; 1.
DR   PANTHER; PTHR22602:SF0; TRANSFERASE CAF17, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR22602; UNCHARACTERIZED; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   PIRSF; PIRSF006487; GcvT; 1.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000313|EMBL:EDZ40077.1};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Transferase {ECO:0000313|EMBL:EDZ40077.1};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          5..228
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          256..321
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   334 AA;  37422 MW;  06519E024DB25CAE CRC64;
     MQTEVSDTRI AHKKFGLFYP SVSRPSIFIE GEDRKTFLQG IASQDILKQD EKSLSYSFFL
     NPKARILFDA WCGNFEDKIG LFPPAGTREE FINHLKKYLF FRTKAKITDM SEHFREIRLV
     GPETISVLLS LFDNNFSGSS FRMLKNGGYV LIHPTSFQHN LDVGLQADLF IPIDQFETTQ
     KSLEDFTSKK GGVLLSESSY LTYLTEKGIP LFPSELNDSF FPAEAGLDSV GVSYNKGCYV
     GQEPVTRLKF QGHLNRSLAG FSLEGAAFPK MEFPVTLFNP KDGNEAGILT RTSFSDILGS
     GIGLGYLKRN FSENGTELLL PDAQLVRVHS LPFV
//
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