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Database: UniProt
Entry: A0A1H7QJ43_9ACTN
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ID   A0A1H7QJ43_9ACTN        Unreviewed;       372 AA.
AC   A0A1H7QJ43;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-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   ORFNames=SAMN04515665_11368 {ECO:0000313|EMBL:SEL48140.1};
OS   Blastococcus sp. DSM 46786.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1798227 {ECO:0000313|EMBL:SEL48140.1, ECO:0000313|Proteomes:UP000198952};
RN   [1] {ECO:0000313|Proteomes:UP000198952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46786 {ECO:0000313|Proteomes:UP000198952};
RA   Varghese N., Submissions S.;
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: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; FOAO01000013; SEL48140.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7QJ43; -.
DR   STRING; 1798227.SAMN04515665_11368; -.
DR   OrthoDB; 9774591at2; -.
DR   Proteomes; UP000198952; 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   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:SEL48140.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198952};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00259}.
FT   DOMAIN          8..264
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          289..367
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   372 AA;  38622 MW;  1916E4D7DF6FB48D CRC64;
     MTSRTSPLHD RHLGAGAKLA DFSGWSMPIE YAGGGVLAEH AAVRDGVGLF DVSHLGTGTV
     RGAGAAAFVD SCLTNDLSRI GPGQAQYTMC CLPDGEAGAG GVVDDLIVYL HGPDDVLLVP
     NAANAAEVLA RLADAAPPGI EVADRHTEVA VLAVQGPRSL QVLELLGVPG EIGYMSFVTG
     TGGAGAEVTL CRTGYTGEHG YELLVGADRA GEMWDAVLEA GQDLGIRPCG LGARDTLRTE
     MGYPLHGHEL SREISPVQAR AGWAVGWRKP AFWGREALLA EKEAGPVRLL WGLRASGRGI
     PRPGMAVLDG DGAQVGEVTS GTFSPTLRTG IGLALLDVAA GVEEGAPLTL DVRGRREPVE
     VVRPPFVPSH VR
//
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