ID A0A1H1D063_9MICC Unreviewed; 829 AA.
AC A0A1H1D063;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glycine cleavage system T protein (Aminomethyltransferase) {ECO:0000313|EMBL:SDQ69895.1};
GN ORFNames=SAMN04489742_2192 {ECO:0000313|EMBL:SDQ69895.1};
OS Arthrobacter crystallopoietes.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=37928 {ECO:0000313|EMBL:SDQ69895.1, ECO:0000313|Proteomes:UP000181917};
RN [1] {ECO:0000313|EMBL:SDQ69895.1, ECO:0000313|Proteomes:UP000181917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20117 {ECO:0000313|EMBL:SDQ69895.1,
RC ECO:0000313|Proteomes:UP000181917};
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; FNKH01000002; SDQ69895.1; -; Genomic_DNA.
DR RefSeq; WP_074700428.1; NZ_FNKH01000002.1.
DR AlphaFoldDB; A0A1H1D063; -.
DR STRING; 37928.SAMN04489742_2192; -.
DR KEGG; acry:AC20117_06445; -.
DR OrthoDB; 2055370at2; -.
DR Proteomes; UP000181917; 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:SDQ69895.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000181917};
KW Transferase {ECO:0000313|EMBL:SDQ69895.1}.
FT DOMAIN 5..375
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 378..433
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 436..718
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 744..821
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 829 AA; 89481 MW; 9D29291FF3583669 CRC64;
MPSPRVVIIG AGIVGANLAD ELTERGWGDI TVLDQGPIPL TGGSTSHAPG LVFQTNPSKA
MTEFAAYTGQ KLASLARGGA RAFNRVGGLE VATTPERLAE IKRRCGFATA WGLEARVVDA
AEAKALHPLI DEDLVLGGLY LPGDGLASSV LAVELLRERA ESRGARFIGG TPVTGIERAA
GRVTGVRSHD TVFPADIVVS AAGFWGPAVG DLIGMPVPLV PLAHQYVTTT PLAELPAAAD
KVIGSGNNAV LPLLRHQDED LYFRQQGARL GIGSYAHRPI AVGYNELPGG PISEHAMPSR
LAFTAEDFEQ PWKACRQLLP GLQETGIEDA FNGIFSFTPD GGSLVGESRD LKGVFIAEAV
WVTHSAGIAK AVAELLVTGR SETDLRELDV ARFEEIQLQP EYVLETSKQN FVEIYDIRHP
LEPRLSPRDL RLSPFHQRQT ELGAFFLETG GWERPHWYEA NASLLDTLPQ DWQPPARDAW
SAKFDSPIAA AEAHATRTNV AMYDMTALKR LEVSGPGALP LLQRLTTGQL DKSIGSVTYT
LMLDDAGGIK SDLTVARIEE TLFQIGANGG LDLDYISRQA AAQTETDPHR WVHVQDTTGG
TCCIGVWGPR ARDLVQPLTP QDLSNDGLKY FRAASTTIAG IPVRLMRLSY VGELGWEIYT
SAEYGLRLWD ALWAAGEPLN VVAAGRSAFN SLRLEKGYRS WGTDMDTEHD PVQAGLAFAV
RGNKDGYVGK AALEQRTAQP PATRLRCLTI DDGTSMVLGK EPVFANGKRA GYVTSAAYGH
TVHKPVAYAW LPGTMDEGDQ VEIEYFGQRI SATVASEPLV DPEMKKIRA
//
