GCST_STAES
ID GCST_STAES Reviewed; 363 AA.
AC Q8CSF4;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Aminomethyltransferase {ECO:0000255|HAMAP-Rule:MF_00259};
DE EC=2.1.2.10 {ECO:0000255|HAMAP-Rule:MF_00259};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000255|HAMAP-Rule:MF_00259};
GN Name=gcvT {ECO:0000255|HAMAP-Rule:MF_00259}; OrderedLocusNames=SE_1222;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000255|HAMAP-Rule:MF_00259}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-
CC aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-
CC 5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] +
CC NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938, ChEBI:CHEBI:57453,
CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00259};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000255|HAMAP-Rule:MF_00259}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000255|HAMAP-
CC Rule:MF_00259}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE015929; AAO04821.1; -; Genomic_DNA.
DR RefSeq; NP_764777.1; NC_004461.1.
DR RefSeq; WP_001831107.1; NZ_WBME01000008.1.
DR AlphaFoldDB; Q8CSF4; -.
DR SMR; Q8CSF4; -.
DR STRING; 176280.SE_1222; -.
DR EnsemblBacteria; AAO04821; AAO04821; SE_1222.
DR GeneID; 50018660; -.
DR KEGG; sep:SE_1222; -.
DR PATRIC; fig|176280.10.peg.1192; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_9; -.
DR OMA; MPVQYPA; -.
DR Proteomes; UP000001411; Chromosome.
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; 3.30.1360.120; -; 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 PANTHER; PTHR43757; PTHR43757; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; SSF101790; 1.
DR TIGRFAMs; TIGR00528; gcvT; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Transferase.
FT CHAIN 1..363
FT /note="Aminomethyltransferase"
FT /id="PRO_0000122601"
SQ SEQUENCE 363 AA; 40421 MW; 9414EBF8DBF4FB9B CRC64;
MTTDLKKTPL YQNYVDSGAK IVEFGGWAMP VQFSSIKEEH NAVRYNVGLF DVSHMGEIEI
SGKDAEQFIQ YILSNDTNLL TNDKAMYSAL CNDEGGIIDD LVTYKLNENH YLLIVNAANT
NKDYQWIKKH SSNFTVDVSN TSDKYGQLAI QGPHSRALIN ELVDIDVSHM AMFEFKQNVQ
IFGKSIILSQ SGYTGEDGFE IYCKQEDTKD IWEQLLEYDV TPCGLGARDT LRLEAGLPLH
GQDLSESITP YEGGIAFAAK PLIENHFIGK SVLKAQKENG SERRTVGLEL LGKGIARTGY
DVLDENSNEI GFVTSGTQSP SSGKSIALAI IDRDAFEMGK KVIVQIRKRQ VEAKIVKKNQ
IEK
