GCST_SYNE7
ID GCST_SYNE7 Reviewed; 372 AA.
AC Q31KT1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Synpcc7942_2308;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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; CP000100; ABB58338.1; -; Genomic_DNA.
DR RefSeq; WP_011244104.1; NC_007604.1.
DR AlphaFoldDB; Q31KT1; -.
DR SMR; Q31KT1; -.
DR STRING; 1140.Synpcc7942_2308; -.
DR PRIDE; Q31KT1; -.
DR EnsemblBacteria; ABB58338; ABB58338; Synpcc7942_2308.
DR KEGG; syf:Synpcc7942_2308; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_3; -.
DR OMA; MPVQYPA; -.
DR OrthoDB; 282830at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2308-MON; -.
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..372
FT /note="Aminomethyltransferase"
FT /id="PRO_1000047719"
SQ SEQUENCE 372 AA; 40041 MW; DF965DADEF333F13 CRC64;
MTLTVTVSLL SSPLHSVCTS AGARFTGFAG WELPLQFQGL MQEHLAVRER AGLFDISHMG
KFQLRGSGLR AALQRLLPSD LTTLLPGQAQ YSVLLNEAGG CLDDLIVYWQ GIVDGVEQAF
LIVNAATTDS DRLWLTEHLP PAIALLDLSQ DLALVAIQGP QAIAFLQPLV SCDLAELPRF
SHTVTSIAGQ PAFVARTGYT GEDGCEVMLP PAAAITLWQQ LTAAGVVPCG LGARDTLRLE
AAMPLYGHEL DTDTNPLEAG LGWVVHLDRN PDFLGRDRLV QAKTNGLERR LVGLELPGRN
IARHGYPVAI ADTTVGIVTS GSWSPTLSKA IALAYVPPAL ANLGQELWVE IRGKQVPATV
VKRPFYRGSQ FR