GCST_PSET1
ID GCST_PSET1 Reviewed; 360 AA.
AC Q3IFV9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=PSHAa2475;
OS Pseudoalteromonas translucida (strain TAC 125).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=326442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAC 125;
RX PubMed=16169927; DOI=10.1101/gr.4126905;
RA Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C.,
RA Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT Pseudoalteromonas haloplanktis TAC125.";
RL Genome Res. 15:1325-1335(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; CR954246; CAI87523.1; -; Genomic_DNA.
DR RefSeq; WP_011329123.1; NC_007481.1.
DR AlphaFoldDB; Q3IFV9; -.
DR SMR; Q3IFV9; -.
DR STRING; 326442.PSHAa2475; -.
DR EnsemblBacteria; CAI87523; CAI87523; PSHAa2475.
DR KEGG; pha:PSHAa2475; -.
DR PATRIC; fig|326442.8.peg.2385; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_6; -.
DR OMA; MPVQYPA; -.
DR OrthoDB; 282830at2; -.
DR BioCyc; PHAL326442:PSHA_RS12185-MON; -.
DR Proteomes; UP000006843; Chromosome I.
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..360
FT /note="Aminomethyltransferase"
FT /id="PRO_1000047693"
SQ SEQUENCE 360 AA; 38947 MW; 7501AED34D400EDA CRC64;
MTSKTVLYAK HLEAGAKMVD FHGWEMPINY GSQIEEHNAV RNDAGMFDVS HMTIVDIQGE
QAQAFLQKLV ANDVAKLTVP GKALYTPMLN EQGGVIDDLI IYFFSNTSYR LVVNSATREK
DLAHLAKISA DFAVTVTERN EFGMIAVQGP NAKAKTATLL TAEQNAAIEG MKPFFGVQTG
DLFIATTGYT GEDGYEIVVP KEQAADLWQQ LLDAGVAPAG LGARDTLRLE AGMNLYGLDM
DESVSPLAAN MAWTIAWEPQ SRDFIGRDVL VQQRADQSTD KQVGLVLEEK GILRSGSKVI
VDGGEGVITS GTFSPTLGYS VALARVPRST GDTAQVEMRK KLVTVKVVKP GFVRNGKSIL