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Database: UniProt
Entry: A0A0B3BX18_9PSED
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ID   A0A0B3BX18_9PSED        Unreviewed;       359 AA.
AC   A0A0B3BX18; A0A0B2D4D7;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=PT85_15880 {ECO:0000313|EMBL:KHO63957.1}, SAMN05421672_12819
GN   {ECO:0000313|EMBL:SIR48148.1};
OS   Pseudomonas flexibilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=706570 {ECO:0000313|EMBL:KHO63957.1, ECO:0000313|Proteomes:UP000030980};
RN   [1] {ECO:0000313|EMBL:KHO63957.1, ECO:0000313|Proteomes:UP000030980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14085 {ECO:0000313|EMBL:KHO63957.1,
RC   ECO:0000313|Proteomes:UP000030980};
RA   Shin S.-K., Yi H.;
RT   "Genome sequence of Pseudomonas tuomuerensis JCM 14085.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SIR48148.1, ECO:0000313|Proteomes:UP000186079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29606 {ECO:0000313|EMBL:SIR48148.1,
RC   ECO:0000313|Proteomes:UP000186079};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-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: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; JTAK01000006; KHO63957.1; -; Genomic_DNA.
DR   EMBL; FTMC01000028; SIR48148.1; -; Genomic_DNA.
DR   RefSeq; WP_027590156.1; NZ_JTAK01000006.1.
DR   AlphaFoldDB; A0A0B3BX18; -.
DR   STRING; 706570.PT85_15880; -.
DR   PATRIC; fig|706570.3.peg.1822; -.
DR   OrthoDB; 9774591at2; -.
DR   Proteomes; UP000030980; Unassembled WGS sequence.
DR   Proteomes; UP000186079; 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:SIR48148.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030980};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00259}.
FT   DOMAIN          7..252
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          278..352
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   359 AA;  38930 MW;  F3B36FF20C540621 CRC64;
     MGERTPLYDL HLALGAKMID FSGWEMPLHY GSQVEEHHQV RRECGVFDVS HLCVVDVTGA
     QAQAFLRRLL ANDVARLDAP GSALYSVVLN EQGGIVDDLL VYLTVDGYRL VSNAATRQRL
     ASWLRQQAAS FAVQLRERSD LAILAVQGPD ARARLSAQVT IARAALIKEL KPFQGLEENG
     WFIARTGYTG EDGLEVMLPA SDAADFFNDL VGAGIAPIGL GARDTLRLEA GLGLYGQDMD
     ESVSPLVSNL AWSVAWTPGR DFIGRAALEA ERDLGVARKL VGLVLEERGV LRAHQAVRVE
     GIGEGEITSG SFAPTVGKSI ALARLPMAAG ERAEVEIRGK WHPVRVVNPP FVRHGRILI
//
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