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Database: UniProt
Entry: A0A1H2SFX5_9BACL
LinkDB: A0A1H2SFX5_9BACL
Original site: A0A1H2SFX5_9BACL 
ID   A0A1H2SFX5_9BACL        Unreviewed;       435 AA.
AC   A0A1H2SFX5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Aminomethyltransferase {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|HAMAP-Rule:MF_00259};
DE            EC=2.1.2.10 {ECO:0000256|ARBA:ARBA00012616, ECO:0000256|HAMAP-Rule:MF_00259};
DE   AltName: Full=Glycine cleavage system T protein {ECO:0000256|ARBA:ARBA00031395, ECO:0000256|HAMAP-Rule:MF_00259};
GN   Name=gcvT {ECO:0000256|HAMAP-Rule:MF_00259};
GN   ORFNames=SAMN05444487_102204 {ECO:0000313|EMBL:SDW30531.1};
OS   Marininema mesophilum.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Marininema.
OX   NCBI_TaxID=1048340 {ECO:0000313|EMBL:SDW30531.1, ECO:0000313|Proteomes:UP000198534};
RN   [1] {ECO:0000313|EMBL:SDW30531.1, ECO:0000313|Proteomes:UP000198534}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45610 {ECO:0000313|EMBL:SDW30531.1,
RC   ECO:0000313|Proteomes:UP000198534};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. {ECO:0000256|HAMAP-Rule:MF_00259}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + N(6)-[(R)-S(8)-
CC         aminomethyldihydrolipoyl]-L-lysyl-[protein] = (6R)-5,10-
CC         methylene-5,6,7,8-tetrahydrofolate + N(6)-[(R)-dihydrolipoyl]-L-
CC         lysyl-[protein] + NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475,
CC         Rhea:RHEA-COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57453, ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00001708, ECO:0000256|HAMAP-
CC         Rule:MF_00259};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000256|HAMAP-Rule:MF_00259}.
CC   -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|ARBA:ARBA00008609,
CC       ECO:0000256|HAMAP-Rule:MF_00259}.
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DR   EMBL; FNNQ01000002; SDW30531.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2SFX5; -.
DR   STRING; 1048340.SAMN05444487_102204; -.
DR   Proteomes; UP000198534; Unassembled WGS sequence.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
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; 4.10.1250.10; Aminomethyltransferase fragment; 1.
DR   HAMAP; MF_00259; GcvT; 1.
DR   InterPro; IPR006223; GCS_T.
DR   InterPro; IPR022903; GCS_T_bac.
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   NCBIfam; TIGR00528; gcvT; 1.
DR   PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR   PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   PIRSF; PIRSF006487; GcvT; 1.
DR   SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR   SUPFAM; SSF103025; Folate-binding domain; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW   Rule:MF_00259}; Methyltransferase {ECO:0000313|EMBL:SDW30531.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198534};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00259}.
FT   DOMAIN          86..330
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          354..432
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   435 AA;  47632 MW;  005FA162625779F8 CRC64;
     MAPKEQAHSG ESLRQKDARR TFLWKALGSM ATQGAHPVYS GLTLRYHGQG VDEEAFTPVA
     YAVPILMEVK IMAELKRTSL YPVYKDEAKL VPFGGWELPV QFSGIKREHE AVREKAGLFD
     VSHMGEIEVK GPDAFSLLQR LTTNDLTKVV PGQAQYTAMC YPDGGTVDDL LVYRKGETSF
     LLVVNAANIA KDGEWIEKHV TGEVEVTDIS EKTSQLALQG PLAQSVLQKL TETDLNAIKL
     FRFVEDVELT GVHGLVSRTG YTGEDGFEIY LPAEDASVLW NKILQAGEDV GVIPCGLGAR
     DTLRFEARLA LYGNELSASV SPIEAGIGFA VKPDKGDFIG REVLARQKEE GAPRKLVGLE
     MTGRGIPRSH YSVYRGEEEI GVVTSGTQSP TLQKNVGLAL IKSELAELGQ ELEVEIRGKR
     VAAKIVPTPF YKRSQ
//
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