GCST_RALPJ
ID GCST_RALPJ Reviewed; 375 AA.
AC B2UG80;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=Rpic_3487;
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12J;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) 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; CP001068; ACD28607.1; -; Genomic_DNA.
DR RefSeq; WP_004628681.1; NC_010682.1.
DR AlphaFoldDB; B2UG80; -.
DR SMR; B2UG80; -.
DR STRING; 402626.Rpic_3487; -.
DR PRIDE; B2UG80; -.
DR EnsemblBacteria; ACD28607; ACD28607; Rpic_3487.
DR KEGG; rpi:Rpic_3487; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_4; -.
DR OMA; MPVQYPA; -.
DR OrthoDB; 282830at2; -.
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..375
FT /note="Aminomethyltransferase"
FT /id="PRO_1000114108"
SQ SEQUENCE 375 AA; 40148 MW; 6E8CAE7C9F89D7CA CRC64;
MTLQHTPLNA IHRSLGARMV DFGGWDMPVN YGSQIEEHHA VRQDAGVFDV SHMCVVDLTG
ARVRDFLRGL LANNVDKLQT PGKALYSCML NPKGGVIDDL IVYFFREDWF RLVVNAGTAP
TDLEWIVAQN AAAGTDVTIT PRRSDNNAGA EPLGILAVQG PNARAKTYAA LPGSQAVGDA
LKPFNAGFVT VENVGEIMVA RTGYTGEDGF ELVVPAAQIA GVWERLLQAG VRPAGLGARD
TLRLEAGMNL YGQDMDEHVS PLDAGLAWTV DLQSERDFTG KAALQAGGQR EQFVGLILRD
KGGVLRAHQK VITAAGDGEI TSGTFSPSLS LSIALARLPK EVPVGTDVQV EIRDRKLTAT
VVKLPFVRNG KALVS
