ID A0A2A5NW08_9MICO Unreviewed; 389 AA.
AC A0A2A5NW08;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:PCN49462.1};
GN ORFNames=Csp2054_00405 {ECO:0000313|EMBL:PCN49462.1};
OS Curtobacterium sp. 'Ferrero'.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=2033654 {ECO:0000313|EMBL:PCN49462.1, ECO:0000313|Proteomes:UP000218649};
RN [1] {ECO:0000313|EMBL:PCN49462.1, ECO:0000313|Proteomes:UP000218649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ferrero {ECO:0000313|EMBL:PCN49462.1,
RC ECO:0000313|Proteomes:UP000218649};
RA Osdaghi E., Forero Serna N., Bolot S., Fischer-Le Saux M., Jacques M.-A.,
RA Portier P., Carrere S., Koebnik R.;
RT "High-Quality Draft Genome Sequence of the Curtobacterium sp. Strain
RT 'Ferrero'.";
RL Submitted (SEP-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCN49462.1}.
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DR EMBL; NXIA01000001; PCN49462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5NW08; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000218649; Unassembled WGS sequence.
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 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00259}.
FT DOMAIN 28..285
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 306..383
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 389 AA; 40792 MW; FAA1CA8B6C50F962 CRC64;
MTEGEFHPTT VVGCRRGRGN SAMRSSPLEA AHEAAGATFT DFAGYRMPVR YSSDLAEHHA
VRTAAGVFDL SHMAEIGVTG PDAVAFLDHA LAGTFGAMTV GRAKYSLLLA EDGGILDDLV
VYRTEEHVFL VVANASNRQV AVDALTARAD AFDVQVSDDS DTTALVAIQG PAAAGTLDAL
VVADRLQPET PLDELRYYRV LHALFDGAEV LVARTGYTGE DGFEIYSDPS IAGDIWDALL
QTGADRGVVP AGLAARDTLR LEAGMPLYGH ELGTDVRPAQ AGLSRVVATS GSFVGDSGVE
PAPGARVLVG LVTEGRRAPR AGYDVVHEGQ VVGTVTSGAL SPTLGHPVAM AFVDPDLATE
GQLLHIDVRG TAIPSTVTPF PFYRRSPRG
//
