ID A0A061M4T1_9BRAD Unreviewed; 817 AA.
AC A0A061M4T1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Aminomethyltransferase {ECO:0000313|EMBL:GAJ37563.1};
GN ORFNames=BDOA9_0201810 {ECO:0000313|EMBL:GAJ37563.1};
OS Bradyrhizobium sp. DOA9.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1126627 {ECO:0000313|EMBL:GAJ37563.1};
RN [1] {ECO:0000313|EMBL:GAJ37563.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DOA9 {ECO:0000313|EMBL:GAJ37563.1};
RX PubMed=25710540; DOI=10.1371/journal.pone.0117392;
RA Okazaki S., Noisangiam R., Okubo T., Kaneko T., Oshima K., Hattori M.,
RA Teamtisong K., Songwattana P., Tittabutr P., Boonkerd N., Saeki K.,
RA Sato S., Uchiumi T., Minamisawa K., Teaumroong N.;
RT "Genome Analysis of a Novel Bradyrhizobium sp. DOA9 Carrying a Symbiotic
RT Plasmid.";
RL PLoS ONE 10:e0117392-e0117392(2015).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; DF820426; GAJ37563.1; -; Genomic_DNA.
DR RefSeq; WP_025038464.1; NZ_DF820426.1.
DR AlphaFoldDB; A0A061M4T1; -.
DR STRING; 1126627.BDOA9_0201810; -.
DR eggNOG; COG0404; Bacteria.
DR OrthoDB; 9804379at2; -.
DR Proteomes; UP000066441; Unassembled WGS sequence.
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; IPR028896; GCST/YgfZ/DmdA.
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; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF9; SARCOSINE DEHYDROGENASE; 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:GAJ37563.1};
KW Transferase {ECO:0000313|EMBL:GAJ37563.1}.
FT DOMAIN 11..366
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 369..424
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 426..698
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 724..809
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 817 AA; 89755 MW; 8A2FD1366C9F3DD1 CRC64;
MAARIPGNAE VVVIGGGIAG CSVAYHLTKL GVSDVVLLER KQLTSGTTWH AAGLVTQLRA
TRNMTELAKY TGELFHSLGP ETGQETGFKQ NGALRIAKSP GRLEELLRGA SMGRNFGLEM
HAVSPAQIKE RWPLLNLDGI MGGIWAPKDG QVNPADVTQA FAKGARMGGA KIVENLRVDR
ILIEHGRAAG VSTNEGDIRA KKVVICGGMW SREFASKHGV SLPLHAAEHF YVVTDAIREL
PRDLPVLFVT DEETYYKEDA GKLLVGCFEK QAKPWARDGI PADFCFDSLP EDFDHFERIL
EMAVNRVPVL ANTGIQLFFN GPESFTPDNR YLLGETSEVS GLFTACGFNS VGILSSGGVG
KALASWVKEG HAPVDLADVD VLRMHPFQSN KTYLYDRTKE ALGLLFDMHW PYRQYTTARD
VRQSVFHDRL KAFGAVMTEA AGWERPGYFS CDGREKEIKY SYGRQNWFDI VGQECRNAAE
RVALFDQSCF VKYMVGGRDA CAALNRICAN NVDVPAGKLV YTQCLNERGG IEADVTVTRL
AEDSYLVVTS ATSQIRDFVW LRRNVSDGAH VFVQDVTSGL PMLGLMGPHA RPLLEHLSGS
DLSNSAFPFA SSREIEIGYA KLRASRVTYV GELGWELYVP AEFAAHVFDR IVEAGADYGL
SQAGYFALGS MRMEKGYRHW GHDIGPEDTP YQAGLGFAVK LEKPQGFIGR EALLRQKEQG
SVRRRLVQFR MIDADAPLVY HQEPVWADGR LVGSITSGAY GHRVGASLAM GYVENGDGVD
ASFLSTSKFE IEVAGRRHRA SAQFAAHYDP SNSKILA
//