ID   B6B7L9_9RHOB            Unreviewed;       816 AA.
AC   B6B7L9;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Glycine cleavage T-protein (Aminomethyl transferase) {ECO:0000313|EMBL:EDZ46610.1};
GN   ORFNames=RBY4I_1826 {ECO:0000313|EMBL:EDZ46610.1};
OS   Rhodobacterales bacterium Y4I.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX   NCBI_TaxID=439496 {ECO:0000313|EMBL:EDZ46610.1, ECO:0000313|Proteomes:UP000005133};
RN   [1] {ECO:0000313|EMBL:EDZ46610.1, ECO:0000313|Proteomes:UP000005133}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4I {ECO:0000313|EMBL:EDZ46610.1,
RC   ECO:0000313|Proteomes:UP000005133};
RA   Moran M.A., Buchan A., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; DS995281; EDZ46610.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6B7L9; -.
DR   STRING; 439496.RBY4I_1826; -.
DR   eggNOG; COG0404; Bacteria.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_11_0_5; -.
DR   OrthoDB; 7156675at2; -.
DR   Proteomes; UP000005133; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; 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   Reference proteome {ECO:0000313|Proteomes:UP000005133};
KW   Transferase {ECO:0000313|EMBL:EDZ46610.1}.
FT   DOMAIN          9..370
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          373..427
FT                   /note="FAD dependent oxidoreductase central"
FT                   /evidence="ECO:0000259|Pfam:PF16350"
FT   DOMAIN          431..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;  89528 MW;  1A3DCB9AD1757A1B CRC64;
     MSDLPNKARV VIIGGGVIGC SVAYHLTKLG WKDVVLLERK QLTSGTTWHA AGLIGQLRAS
     SNMTKLARYS AELYLGLEAE TGVATGMRQV GSVSAALTHE RLEELYRNAA MARAFGVPVE
     ELSPKEVKER YEHINLDGVT GGVWLPTDGQ ADPANIALAL AKGARQRGAL VKERIKVTGI
     AKQGRRITGV DWVSDDGGAQ GHIECDMVVN CAGMWGHEVG RMAGVNVPLH ACEHFYIVTE
     GIEGLTQMPV LRVPDECAYY KEDAGKILLG AFEPNAKPWA MNGIPDSFEF DQLPEDFDHF
     EPILEAACNR MPMLAEAGIH TFFNGPESFT PDDAYHLGLA PEMDNFWVAA GFNSIGIQSA
     GGAGMALAQW MEDGQKPFDL GDVDISRMHP FQGNKHYLFE RSKETLGLLY ADHFPYRQKA
     TARGVRRTPF HHHLKEQGAV FGEIGGWERA NWFANAGQER EYEYSWKRQN WFENSAAEHR
     AVRENVGMYD MSSFGKIRVE GPDAEKFLNY ICGANVSVPA GKIVYTQFLN PRGGIEADVT
     VTRLSETAYL VVTPAVTRLA DQTWMMRNKG GFNVVLTDVT AGEGVLAVMG PNARKLLQRV
     SPNDFSNEVN PFGTAQEIEL GMGLARVHRV TYVGELGWEI YIPAEMSGHA FETLWEAGQD
     MGLKLCGMHM MDSCRIEKGF RHFGHDITCE DNVIDAGLGF AVATGKDDFI GKAAVLERKE
     TGPKARMVQF KLTDPEPLLF HNEPIIRDGK YVGYLSSGNY GHTLGAAIGM GYVPCEGESA
     ADVLGSTYEI DVCGVKVKAE AALKPMYDPK SERVKA
//