ID A0A0M6XK08_9RHOB Unreviewed; 833 AA.
AC A0A0M6XK08;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Aminomethyltransferase {ECO:0000313|EMBL:CTQ31439.1};
DE EC=2.1.2.10 {ECO:0000313|EMBL:CTQ31439.1};
GN Name=gcvT_1 {ECO:0000313|EMBL:CTQ31439.1};
GN ORFNames=JAN5088_00197 {ECO:0000313|EMBL:CTQ31439.1};
OS Jannaschia rubra.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=282197 {ECO:0000313|EMBL:CTQ31439.1, ECO:0000313|Proteomes:UP000048908};
RN [1] {ECO:0000313|EMBL:CTQ31439.1, ECO:0000313|Proteomes:UP000048908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5088 {ECO:0000313|EMBL:CTQ31439.1,
RC ECO:0000313|Proteomes:UP000048908};
RA Noorani M.;
RL Submitted (JUL-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; CXPG01000009; CTQ31439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M6XK08; -.
DR STRING; 282197.SAMN04488517_101220; -.
DR Proteomes; UP000048908; 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: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.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000313|EMBL:CTQ31439.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000048908};
KW Transferase {ECO:0000313|EMBL:CTQ31439.1}.
FT DOMAIN 9..381
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 385..437
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 440..722
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 744..823
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 833 AA; 92620 MW; 09BEAA7BE308BB4E CRC64;
MRMKTHVRAL VVGGGAVGTS IAYHLAKAGW DTMLLERDEL TSGSTWHAAG LLPYFNMGYA
TSHIHDYSIR FYKTLEEETG LNPGFSVVGN LRMAQTQARM DEYELYASLA ETVGIPHEWL
TPADIADRYP LVRTDDLVGA ILHPTDGYIN PADVTMAMAR GARQHGATIE RRWQVDGYHW
TGEHWDVTAT RMVERGGNLV ASDEQVTIHA EHVVTATGNH AQRTAQLLGI KTPAIVVEHQ
YIVTEPDPAL VEWRKSNPQH PVLRDADAKW YVREERGGWI LGPYEQNAPA RFPFGVPDSF
RADLFPLDLE RIEQEYMSFI HRIPSSENAG LKDDFNGPIC YTPDGNPLVG PAPGLRNMWL
AEGFSFGITA AGGTGHYLAQ MMTSGEAEID MASLDPRRFG KWMTTEYAMR KNEEAYDHVY
VLHHPDEERP ACRPLKTAPC YDRMKARGAQ FGCVNGWERP NYFGPLDAPD SFDHDSRSFR
RGAWWGHAVT EAKAIREGVG MIDATAFTKH MLRGPGAAAF LDWFTTNKLP KVGRINLTYA
LTEAGTTRTE YTIVRLAEDT FYLVSAGAWQ AYDSDFLAKA VNDKVNDFGP MWLDDCTGAH
GVFALAGPRA RDVLRDLIVA PDPTFALSNK GFPWLSARRI ELGMVPVNAI RVAYTGELGW
ELHHPMEMQN HLFDRLMAAG EAHGLTLVGA RAQNWLRQEK SYRAFGTELG RDATPLEAGL
DRFVDLSKDF HGKAAMEETG IRSKCVTLLI DGPDDADPWG REALYAGDDR VGRLTSGGYS
VAFGRSIGMG YVRPDLAVPG TPLQVRMQRA LWEAEVTEDS PYDPTNARIR ADG
//