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Database: UniProt
Entry: A0A024GX82_9MICC
LinkDB: A0A024GX82_9MICC
Original site: A0A024GX82_9MICC 
ID   A0A024GX82_9MICC        Unreviewed;       377 AA.
AC   A0A024GX82;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
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:CCQ44545.1};
GN   ORFNames=ARTSIC4J27_471 {ECO:0000313|EMBL:CCQ44545.1};
OS   Pseudarthrobacter siccitolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Pseudarthrobacter.
OX   NCBI_TaxID=861266 {ECO:0000313|EMBL:CCQ44545.1, ECO:0000313|Proteomes:UP000035722};
RN   [1] {ECO:0000313|Proteomes:UP000035722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4J27 {ECO:0000313|Proteomes:UP000035722};
RX   PubMed=24948757; DOI=10.1128/genomeA.00526-14;
RA   Manzanera M., Santa-Cruz-Calvo L., Vilchez J.I., Garcia-Fontana C.,
RA   Silva-Castro G.A., Calvo C., Gonzalez-Lopez J.;
RT   "Genome Sequence of Arthrobacter siccitolerans 4J27, a Xeroprotectant-
RT   Producing Desiccation-Tolerant Microorganism.";
RL   Genome Announc. Announc.2:e00526-e00514(2014).
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:CCQ44545.1}.
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DR   EMBL; CAQI01000027; CCQ44545.1; -; Genomic_DNA.
DR   RefSeq; WP_050053606.1; NZ_CAQI01000027.1.
DR   AlphaFoldDB; A0A024GX82; -.
DR   STRING; 861266.ARTSIC4J27_471; -.
DR   OrthoDB; 9774591at2; -.
DR   Proteomes; UP000035722; 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          8..265
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          296..374
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   377 AA;  40001 MW;  1605981FD0DD21EF CRC64;
     MTENYTALYE QHKIAGASFT DFGGWQMPLK YNSELAEHRA VRKAAGLFDL SHMGEVWVTG
     PDAAAFLDYA LVGKLSAVAV GKAKYSLICQ EDGGIIDDLI SYRLDEQKYL VIPNAGNAAV
     VAAALAERAA NFDVTVEDVS AETSLIAVQG PTAEAILLKL VPAAQHPLVT ELKYYAAVEV
     GITVNGTVQE LLLARTGYTG EDGFEIYIPN EDAAGLWEAL LEVGAGHGLI PAGLACRDSL
     RLEAGMPLYG NELSRDGNPY AAGLGPVVSL KKESNFVGRA VLAELKELGA GSTSGRKLVG
     LKGLGRRAGR SHYPVLKDGT VVGEVTSGQP SPTLGYPIAL AYVDVEHSAP GTALDIDLRG
     KAEPFEVVKL PFYKRQK
//
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