ID A0A0P1IQT3_9RHOB Unreviewed; 805 AA.
AC A0A0P1IQT3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Aminomethyltransferase {ECO:0000313|EMBL:CUJ95584.1};
DE EC=2.1.2.10 {ECO:0000313|EMBL:CUJ95584.1};
GN Name=gcvT_10 {ECO:0000313|EMBL:CUJ95584.1};
GN ORFNames=PH7735_01888 {ECO:0000313|EMBL:CUJ95584.1};
OS Shimia thalassica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1715693 {ECO:0000313|EMBL:CUJ95584.1, ECO:0000313|Proteomes:UP000051870};
RN [1] {ECO:0000313|Proteomes:UP000051870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7735 {ECO:0000313|Proteomes:UP000051870};
RA Rodrigo-Torres Lidia, Arahal R.David.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; CYTW01000001; CUJ95584.1; -; Genomic_DNA.
DR RefSeq; WP_058310966.1; NZ_CYTW01000001.1.
DR AlphaFoldDB; A0A0P1IQT3; -.
DR STRING; 1715693.PH7735_01888; -.
DR GeneID; 83880926; -.
DR Proteomes; UP000051870; Unassembled WGS sequence.
DR GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
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 PANTHER; PTHR13847:SF187; DIMETHYLGLYCINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:CUJ95584.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051870};
KW Transferase {ECO:0000313|EMBL:CUJ95584.1}.
FT DOMAIN 6..367
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 370..423
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 427..692
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 718..797
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 805 AA; 88593 MW; D42337F6985A0E3C CRC64;
MKTTTRVVVI GGGVVGCSVL YHLTKLGWSD VMLLERSELT SGSTWHAAGG FHTLNGDTNM
AALQGYTIKL YKELEEITGM SCGLHHVGGV TLADNQERFD MLVAERAKHR FMGLDTEIVT
PEEIKKIAPV TNTDGIIGGL YDPLDGHLDP SGTTHAYAKA ARMGGATIET HCMVKETNQR
PDGTWDVVTD KGTIHAEHIV NAGGLWAREV GAMAGVYMPL HPMEHIYLVT DEVPMIAEII
DGGGEHPHVM DPAGESYLRQ EGRGLCIGFY EQPCKPWAVE GTSWDFGHEL LPDNFDKIED
SIDFAYKRFP ALEAAGIKSS IHGPFTFAPD GNPLVGPVPG MRNYWSACGV MAGFSQGGGV
GLMLAQWMVE GECERDTMAM DIARFGDWIT PGYTLPKVIE NYQKRFSVSY PNEELPAARP
FRTTPMYDIF DNMGAVWGAQ YGLEVANYFA EGDEPRFETP SFRRSNAFEA TAREVKAVRE
AVGINETHNF GKYLVSGAGA RAWLDRIMAG RVPKPGRLSL TPMLSPKGRL IGDFTISCLS
ETEFQLTASY GSQSYHMRWF QQNLDDGVAL QNISDTRNGF QIAGPMARDV LQACTRQDIS
DMKFMDVRRM TVGMADCIVQ RVSYTGDLGY EIYCDLPSQR ALWDVLWTAG QPHGMKPFGM
RAMMSLRLDK FFGSWLSEFS PDYTAAETGL DRFISFKKNT SFIGRAAAEA ERDAGATRKL
CAFEVDAVDA DVNAYEPIWL DGAVVGFCTS GGYSHHAQKS IAQGFVPTDR AVEGLEVEIE
ILGSMCKARL ITTPLFDEDG SRMRG
//