ID   A0A0P1ILA2_9RHOB        Unreviewed;       816 AA.
AC   A0A0P1ILA2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Aminomethyltransferase {ECO:0000313|EMBL:CUK24377.1};
DE            EC=2.1.2.10 {ECO:0000313|EMBL:CUK24377.1};
GN   Name=gcvT_1 {ECO:0000313|EMBL:CUK24377.1};
GN   ORFNames=TA5114_00160 {ECO:0000313|EMBL:CUK24377.1};
OS   Cognatishimia activa.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cognatishimia.
OX   NCBI_TaxID=1715691 {ECO:0000313|EMBL:CUK24377.1, ECO:0000313|Proteomes:UP000051184};
RN   [1] {ECO:0000313|Proteomes:UP000051184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5114 {ECO:0000313|Proteomes:UP000051184};
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; CYUE01000002; CUK24377.1; -; Genomic_DNA.
DR   RefSeq; WP_058313395.1; NZ_CYUE01000002.1.
DR   AlphaFoldDB; A0A0P1ILA2; -.
DR   STRING; 1715691.TA5113_00785; -.
DR   OrthoDB; 7156675at2; -.
DR   Proteomes; UP000051184; 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:UniProtKB-KW.
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:SF193; PYRUVATE DEHYDROGENASE PHOSPHATASE REGULATORY SUBUNIT, 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:CUK24377.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051184};
KW   Transferase {ECO:0000313|EMBL:CUK24377.1}.
FT   DOMAIN          9..370
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          373..428
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          430..701
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          726..808
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   816 AA;  89771 MW;  D9719FA4A4B1EE57 CRC64;
     MSDIPAKARV VIVGGGVIGC SVAYHLAKKG WTDVVLLERK QLTSGTTWHA AGLIAQLRAT
     KNMTKLAKYS QELYGTLEEE TGVATGFKRN GSITVALTEE RKEEIYRQAA MARAFGVEVE
     EISNERVLEM YPHINLDGIK GAVYLPLDGQ GDPGNIALAL AKGAKQNGAL VKERTKVTGF
     VKEGRKVTGV EWESDDGSAS GTIECDMVVN CGGMWGREVG KMAGVNVPLQ ACEHFYIVTE
     NIEGMSQLPV LRVPDEYAYY KEDAGKILLG AFEPEAKPWA VDGIPSDFEF DQLPEDFDHF
     EPILEMAVER MPILAEAGIH TFFNGPESFT PDDAYHLGLA PEMDNVWVAA GFNSIGIQSA
     GGAGLALSEW MTTGERPFDL GDVDIARMQP FQNNGKYLEE RSRETLGLLY KDHFPFKQKE
     TARGVRRSPL HHHLLENGAV MGEFAGWERA NWIADAGQEA EYKYSWKRQN FFGNVAQEHK
     AIRENVGMYD MSSFGKIRVE GPDATAYMNY VGGGQYDVPV GKIVYTQFLN RTGGIEADVT
     VTRLSETAYL VVTPAATRQA DQTWMMRNKG DFNVVITDVT PGEAVLAVMG PNSRKLLEMV
     SPNDFSNAVN PFGTAQEIEL GMGLARVHRV TYVGELGWEV YVSSDMAGHA FETLWEAGQD
     LDLKLCGMHM MDTCRIEKGF RHFGHDITCE DHVIDAGLGF AVKTDKPDFI GRDAVLQRKE
     TGPQNRMLQF KLTDSEPLLY HNEPILRDGE VVSYLTSGAY GHHLGGAIGL GYVPCAGEKA
     ADVLASTYEI DVMGTRVKAE ASLKPMYDPT SERVKA
//