GCST_XYLF2
ID GCST_XYLF2 Reviewed; 368 AA.
AC B2I6Q1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=XfasM23_0136;
OS Xylella fastidiosa (strain M23).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405441;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M23;
RX PubMed=20601474; DOI=10.1128/jb.00651-10;
RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT causing almond leaf scorch disease in California.";
RL J. Bacteriol. 192:4534-4534(2010).
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; CP001011; ACB91593.1; -; Genomic_DNA.
DR RefSeq; WP_004087174.1; NC_010577.1.
DR AlphaFoldDB; B2I6Q1; -.
DR SMR; B2I6Q1; -.
DR EnsemblBacteria; ACB91593; ACB91593; XfasM23_0136.
DR GeneID; 58015706; -.
DR KEGG; xfn:XfasM23_0136; -.
DR HOGENOM; CLU_007884_10_2_6; -.
DR OMA; MPVQYPA; -.
DR Proteomes; UP000001698; 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..368
FT /note="Aminomethyltransferase"
FT /id="PRO_1000114126"
SQ SEQUENCE 368 AA; 41076 MW; 6F89AC53877AAF70 CRC64;
MIKKTILNDT HQALGAKMVD FSGWEMPIHY GSQIDEHHHV RRNAGIFDVS HMTVIDLHGT
QVRPLLRRLL ANSVDKLKVP GKALYSCMLN PQGGVIDDLI VYYLREDYFR FIVNAATREK
DLAWINTQAS AFNVRVEERA DLAMLAVQGP AARAQVTNLL AETHRDAVEK LGRFAALEVA
SHSKKPLFIS RTGYTGEDGF EILLPQEETI TLWNALLKTG VKPIGLGARD TLRLEAGMNL
YGQDMDEQVS PYEAALGWTV MLDEGRNFIG RNVLEQQKTN GVSRQMIGLL MDEKGVLRHG
QKVLTAQGEG HILSGTFSPT LNKAIGFARV PAGKPSEVRV NIRDREIPVR VVKFPFVREG
QTQPNIFD