GCST_SHESA
ID GCST_SHESA Reviewed; 364 AA.
AC A0L105;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 85.
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};
GN OrderedLocusNames=Shewana3_3501;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000469; ABK49724.1; -; Genomic_DNA.
DR RefSeq; WP_011718288.1; NC_008577.1.
DR AlphaFoldDB; A0L105; -.
DR SMR; A0L105; -.
DR STRING; 94122.Shewana3_3501; -.
DR EnsemblBacteria; ABK49724; ABK49724; Shewana3_3501.
DR KEGG; shn:Shewana3_3501; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_6; -.
DR OMA; MPVQYPA; -.
DR OrthoDB; 282830at2; -.
DR Proteomes; UP000002589; 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..364
FT /note="Aminomethyltransferase"
FT /id="PRO_1000047704"
SQ SEQUENCE 364 AA; 39649 MW; 5ADD7B226FD4F525 CRC64;
MANKTVLFNK HLESNAKMVD FHGWDMPLNY GSQIEEHHAV RQDAGMFDVS HMTVVDVTGT
DACAFLRKLL ANDVAKLKVP GKALYGGMLD DNAGIIDDLI TYYLTDTFYR VVVNSATREK
DLAWIAKQSQ GFDVTVTERP ELAMIAVQGP NAKAKAAAVF SADQNAAIEG MKPFFGKQAG
SLFIATTGYT GEVGYEIIVP ETEAEALWQA LLDQGVKPCG LGARDTLRLE AGMNLYGLDM
DETINPLAAN MGWTIAWEPT DRDFIGRQAL EALRDAGTDK LVGLVMEEKG VLRHDMPVFF
TDAAGVEQQG VITSGTFSPT LGYSIAMARV PNSIGDTAEV EMRKKRVAVR VVAPNFVRNG
KQAF
