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Database: UniProt
Entry: A0A0G3H5V1_9CORY
LinkDB: A0A0G3H5V1_9CORY
Original site: A0A0G3H5V1_9CORY 
ID   A0A0G3H5V1_9CORY        Unreviewed;       365 AA.
AC   A0A0G3H5V1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
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   ECO:0000313|EMBL:AKK06532.1};
GN   ORFNames=CMUST_11085 {ECO:0000313|EMBL:AKK06532.1};
OS   Corynebacterium mustelae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=571915 {ECO:0000313|EMBL:AKK06532.1, ECO:0000313|Proteomes:UP000035199};
RN   [1] {ECO:0000313|EMBL:AKK06532.1, ECO:0000313|Proteomes:UP000035199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45274 {ECO:0000313|EMBL:AKK06532.1,
RC   ECO:0000313|Proteomes:UP000035199};
RX   PubMed=26358597;
RA   Ruckert C., Eimer J., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of the Type Strain Corynebacterium mustelae DSM
RT   45274, Isolated from Various Tissues of a Male Ferret with Lethal Sepsis.";
RL   Genome Announc. 3:e01012-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000035199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45274 {ECO:0000313|Proteomes:UP000035199};
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete genome sequence of Corynebacterium mustelae DSM 45274, isolated
RT   from various tissues of a male ferret with lethal sepsis.";
RL   Submitted (MAY-2015) 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:ARBA00043710, 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; CP011542; AKK06532.1; -; Genomic_DNA.
DR   RefSeq; WP_047262547.1; NZ_CP011542.1.
DR   AlphaFoldDB; A0A0G3H5V1; -.
DR   STRING; 571915.CMUST_11085; -.
DR   KEGG; cmv:CMUST_11085; -.
DR   PATRIC; fig|571915.4.peg.2363; -.
DR   OrthoDB; 9774591at2; -.
DR   Proteomes; UP000035199; Chromosome.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:UniProtKB-UniRule.
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   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}; Reference proteome {ECO:0000313|Proteomes:UP000035199};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00259}.
FT   DOMAIN          9..260
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          282..360
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   365 AA;  38677 MW;  62D1C3EF2994BDE8 CRC64;
     MTDLRQSPLH AEHEKLGATF IPFGPWNMPL KYGNELAEHR AVRGTCGIFD LSHMGEVWVK
     GPDAGAFLDY ALISRLSTIK VGKAKYTMIV AASGGIIDDL IVYRTDLDTF LVVPNAGNAE
     VVAKELQDRA AGFDVALDDA SAATALIAVQ GPNAQALILE LAADPQTVTE LGYYAAVPAV
     IADHDVLLAR TGYTGEDGFE LFIPAEKATD LWQKITAAGG PHELVPCGLA ARDSLRLEAG
     MPLYGNELTL QTTPLHAGLS VLVAKEGDFI GKDALSTVSP ERVLVGLSSS GRRAARSHAL
     LFDATGTEVG EVTSGQPSPT LGHPIALAYV DVAHSDSGTA LEAEISGKRY PFEVVALPFY
     SRKRT
//
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