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Database: UniProt
Entry: C4KBM4_THASP
LinkDB: C4KBM4_THASP
Original site: C4KBM4_THASP 
ID   C4KBM4_THASP            Unreviewed;       363 AA.
AC   C4KBM4; A0A5C7SZN2;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 85.
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:TXH88822.1};
GN   OrderedLocusNames=Tmz1t_3205 {ECO:0000313|EMBL:ACR01800.1};
GN   ORFNames=E6Q80_04785 {ECO:0000313|EMBL:TXH88822.1};
OS   Thauera aminoaromatica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=164330 {ECO:0000313|EMBL:ACR01800.1, ECO:0000313|Proteomes:UP000002186};
RN   [1] {ECO:0000313|Proteomes:UP000002186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MZ1T {ECO:0000313|Proteomes:UP000002186};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sayler G.S.;
RT   "Complete sequence of chromosome of Thauera sp. MZ1T.";
RL   Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR01800.1, ECO:0000313|Proteomes:UP000002186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MZ1T {ECO:0000313|EMBL:ACR01800.1,
RC   ECO:0000313|Proteomes:UP000002186};
RX   PubMed=23407619; DOI=10.4056/sigs.2696029;
RA   Jiang K., Sanseverino J., Chauhan A., Lucas S., Copeland A., Lapidus A.,
RA   Del Rio T.G., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D.,
RA   Brettin T., Detter J.C., Han C., Chang Y.J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N.C., Mikhailova N., Moser S., Jegier P., Close D.,
RA   Debruyn J.M., Wang Y., Layton A.C., Allen M.S., Sayler G.S.;
RT   "Complete genome sequence of Thauera aminoaromatica strain MZ1T.";
RL   Stand. Genomic Sci. 6:325-335(2012).
RN   [3] {ECO:0000313|EMBL:TXH88822.1, ECO:0000313|Proteomes:UP000321192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bin_27_1 {ECO:0000313|EMBL:TXH88822.1};
RA   Stamps B.W., Spear J.R.;
RT   "Metagenome Assembled Genomes from an Advanced Water Purification
RT   Facility.";
RL   Submitted (SEP-2018) 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; CP001281; ACR01800.1; -; Genomic_DNA.
DR   EMBL; SSFD01000065; TXH88822.1; -; Genomic_DNA.
DR   RefSeq; WP_004312585.1; NZ_SSFD01000065.1.
DR   AlphaFoldDB; C4KBM4; -.
DR   STRING; 85643.Tmz1t_3205; -.
DR   KEGG; tmz:Tmz1t_3205; -.
DR   eggNOG; COG0404; Bacteria.
DR   HOGENOM; CLU_007884_10_2_4; -.
DR   OrthoDB; 9774591at2; -.
DR   Proteomes; UP000002186; Chromosome.
DR   Proteomes; UP000321192; 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:TXH88822.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002186};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00259}.
FT   DOMAIN          10..258
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          282..356
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   363 AA;  38872 MW;  A65F21193630A7AE CRC64;
     MTIAAKQTPL HAAHVAAGAR MVDFAGWDMP VNYGSQIEEH HAVRRDAGMF DVSHMLALDL
     AGPDATTWLR GLLANDVAKL KDNGKALYSC MLNERGGVID DLIVYRFSDA DYRIVVNAGT
     ADKDVAWMRQ RIAATGANVT LQARRDLAMI AVQGPRAIER ATLALPELST ANGVPAPFFG
     ARVGDLLIAR TGYTGEDGLE IAVPASRAEA MWNALAAAGV RPCGLGARDT LRLEAGMNLY
     GQDMDDHVSP LNAGLSWTVD MKDEARDFLG RAALQANPAS QRLLGLILED KGVLRSHMKV
     FTSGGEGETT SGSFSPTLEK SIAFARVPLA TQPGEAVEVD IRGKRLKART VKLPFVRNGK
     ALV
//
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