ID A0A1H1R3G4_9MICO Unreviewed; 860 AA.
AC A0A1H1R3G4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Glycine cleavage system T protein (Aminomethyltransferase) {ECO:0000313|EMBL:SDS30222.1};
GN ORFNames=SAMN04489751_1705 {ECO:0000313|EMBL:SDS30222.1};
OS Brevibacterium sandarakinum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=629680 {ECO:0000313|EMBL:SDS30222.1, ECO:0000313|Proteomes:UP000199700};
RN [1] {ECO:0000313|EMBL:SDS30222.1, ECO:0000313|Proteomes:UP000199700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22082 {ECO:0000313|EMBL:SDS30222.1,
RC ECO:0000313|Proteomes:UP000199700};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; LT629739; SDS30222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1R3G4; -.
DR STRING; 629680.SAMN04489751_1705; -.
DR OrthoDB; 2055370at2; -.
DR Proteomes; UP000199700; Chromosome i.
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:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 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:SDS30222.1};
KW Transferase {ECO:0000313|EMBL:SDS30222.1}.
FT DOMAIN 13..383
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 387..441
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 444..727
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 752..852
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 860 AA; 93006 MW; C1481731AE9588C7 CRC64;
MPISSPSSPS SPRVVIIGAG IVGANLADEL AQLGWTNTLV LEQGPLNIPG GSTSHAPGLV
FSSNGSKSMT EFAQYTIEKL TSLTGSDGRG SFLPVGGLEI ATQEDRLQDL HRRAGWNRSW
GVDAEVVDAQ ECLRLFPMLG PDKVLGGLLT PGDGLALAAR GTQLVMDRAR AAGVEFRDRT
TVTGIEQSGG KVTAVLAGDD RFPADIVVSC AGFWGPNIGA MVGTTIPLLP LGHQFAWTTE
VPSLAGKNEQ PARASAPILR YQDKDLYYRE WGERIGIGSY AHRPMPVDLD TLRTYSPDEI
TDEVMPSSLD FTPEDFAREW EATKELLPEL AQTQVQRGFN GIFSFTPDGG SLVGQSREVD
GFFVAEAVWV THGAGIARAV AELIALGRSN TDLSGIDLNR FEDALTTPEY VSETSQQNFV
EIYDVIHPLQ PRVSPRDLRL SPFNDRQKEL GAFFLETNGW ERPHWYEANA SLLEELPEEW
KAPKREGWAD MFHSPIAAVE AWKTRTNVAM YDMTALKRFE VKGPGAGELL HGLTTSSMLR
KPGAVSYTLL LDDEGGITSD ITVAILDEQT YQVGANSNID FATITRAARE QSTADPSKWA
TVRETTQGTC CIGLWGPLAR EVISQVSNDD LSNDGLKYFR TKQITIGGVP VTAMRLSYVG
ELGWELYTSA DLGHRLWDVL WEAGREFGLI AGGREAFNSM RLEKGFRSFG SDMTSEHEPV
QAGLGFAVKA SKTDDFRGKA ALESRAAAAT TKLTCLTLDR REDVVLGSEP VYVAGGSAGR
TDAAGSDHGA SGAVNRSGKA DGYVTSAAYG YSIGQTIAYA WLPNTLSVGD GVEIEYLGRR
LPATVTAEPI FDPEMTRLKG
//