ID A0A1H4NQ23_9MICC Unreviewed; 835 AA.
AC A0A1H4NQ23;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Glycine cleavage system T protein (Aminomethyltransferase) {ECO:0000313|EMBL:SEB97280.1};
GN ORFNames=SAMN04489745_1738 {ECO:0000313|EMBL:SEB97280.1};
OS Arthrobacter woluwensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=156980 {ECO:0000313|EMBL:SEB97280.1, ECO:0000313|Proteomes:UP000182652};
RN [1] {ECO:0000313|EMBL:SEB97280.1, ECO:0000313|Proteomes:UP000182652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10495 {ECO:0000313|EMBL:SEB97280.1,
RC ECO:0000313|Proteomes:UP000182652};
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; FNSN01000003; SEB97280.1; -; Genomic_DNA.
DR RefSeq; WP_066210641.1; NZ_FNSN01000003.1.
DR AlphaFoldDB; A0A1H4NQ23; -.
DR STRING; 156980.SAMN04489745_1738; -.
DR Proteomes; UP000182652; 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: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:SEB97280.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000182652};
KW Transferase {ECO:0000313|EMBL:SEB97280.1}.
FT DOMAIN 6..381
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 384..439
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 442..724
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 749..827
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 835 AA; 91497 MW; F47C3743C8F9FE05 CRC64;
MSTSPRVVII GAGIVGTNLA DELSSRGWTN VTVVEQGPLE LAGGSTSHAP GLVFQNNGSR
TMTQFATYTV EKLLGLSKDG QSCFNQVGGL ELATTPERLK DLHRKMGLMT SWGVESRIID
ADECEKHYPL LTTGALSDGH EILGGLLIPS DGLALAARAV QLLIERASER GVEFRGSTTV
TGIARDGGKV TGVETDAGLI PADIVVSCAG FWGRELGKMV GLEVPLLPLG HQYAVTTPLP
ELEGVNELPK GASKPILRYQ DKDLYYREWG DRIGIGSYAH RPMPVDMTRL PQVSAEEMSD
HKMPSRLDFT LEDFLPAWED SQDLLPALRN AEIEDGFNGI FSFTPDGGPL IGEHPDLSGF
FVAEAVWVTH SAGVAKAVAE LLIEGRSRTD LHGTELTRFE KVQTSDDYVS ETSQQNFVEI
YDILHPLQPK ESPRDLRVSP FHVRQKELGA FFLEASAWER PHWFEANRGL LEELPDEWQA
PERESWSGMF HSPISAAEAW KTRTAVALYD MTPLKRLEVV GPGAEALLHR LSTGNITKKP
GAVTYCLLLE HDGGIRSDVT VARLEDERFQ LGVNSNVDFD YLRAEARRQS AADPSQWAHV
SDITGSTCCI GLWGPLAREV IGKVSDDDLS NDGLKYFRAK EISVGGIPVT AMRLSYVGEL
GWELYTSAEY GLKLWDLLFE AGQEFGIIAA GRGAFNSLRL EKGYRLWGTD MNTEHHPYQA
GLGFSVAKDK VGFTGAEALA ERKEQPAEKT LRCLTIDDGR SVVLGKEPVY VDGEASGYVT
SAAYGFSIHR PIAYAWLPTA VGIGDRVEIE YFGERIPATV TAEPLYDPSM ERIRG
//