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GCST_SHIDS
ID   GCST_SHIDS              Reviewed;         364 AA.
AC   Q32BW7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=SDY_3176;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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}.
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DR   EMBL; CP000034; ABB63188.1; -; Genomic_DNA.
DR   RefSeq; WP_000068707.1; NC_007606.1.
DR   RefSeq; YP_404679.1; NC_007606.1.
DR   AlphaFoldDB; Q32BW7; -.
DR   SMR; Q32BW7; -.
DR   STRING; 300267.SDY_3176; -.
DR   EnsemblBacteria; ABB63188; ABB63188; SDY_3176.
DR   KEGG; sdy:SDY_3176; -.
DR   PATRIC; fig|300267.13.peg.3794; -.
DR   HOGENOM; CLU_007884_10_2_6; -.
DR   OMA; MPVQYPA; -.
DR   Proteomes; UP000002716; 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; Reference proteome; Transferase.
FT   CHAIN           1..364
FT                   /note="Aminomethyltransferase"
FT                   /id="PRO_1000047709"
SQ   SEQUENCE   364 AA;  40177 MW;  EA44EBB25295E33A CRC64;
     MAQQTPLYEQ HTLCGARMVD FHGWMMPLHY GSQIDEHHAV RTDAGMFDVS HMTIVDLRGS
     RTREFLRYLL ANDVAKLTKS GKALYSGMLN ASGGVIDDLI VYYFTEDFFR LVVNSATREK
     DLSWITQHAE PFGIEITVRD DLSMIAVQGP NAQAKAATLF NDAQRQAVEG MKPFFGVQAG
     DLFIATTGYT GEAGYEIALP NEKAADFWRA LVEAGVKPCG LGARDTLRLE AGMNLYSQEM
     DETISPLAAN MGWTIAWEPA DRDFIGREAL EAQREHGTEK LVGLVMTEKG VLRNELPVRF
     TDVQGNQHEG IITSGTFSPT LGYSIALARV PEGIGETAIV QIRNREMPVK VTKPVFVRNG
     KAVA
 
 
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