GCST_BACTN
ID GCST_BACTN Reviewed; 361 AA.
AC Q89YZ6;
DT 30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=BT_4584;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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; AE015928; AAO79689.1; -; Genomic_DNA.
DR RefSeq; NP_813495.1; NC_004663.1.
DR RefSeq; WP_008764743.1; NC_004663.1.
DR AlphaFoldDB; Q89YZ6; -.
DR SMR; Q89YZ6; -.
DR STRING; 226186.BT_4584; -.
DR PaxDb; Q89YZ6; -.
DR PRIDE; Q89YZ6; -.
DR EnsemblBacteria; AAO79689; AAO79689; BT_4584.
DR GeneID; 60925758; -.
DR KEGG; bth:BT_4584; -.
DR PATRIC; fig|226186.12.peg.4664; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_10; -.
DR InParanoid; Q89YZ6; -.
DR OMA; MPVQYPA; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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..361
FT /note="Aminomethyltransferase"
FT /id="PRO_0000122544"
SQ SEQUENCE 361 AA; 39826 MW; C57E87A164F95A89 CRC64;
MKTTPFTEKH IALGAKMHEF AGYNMPIEYS GIIDEHLTVC NAVGVFDVSH MGEFWVKGPQ
ALAFLQKVTS NNVAALVPGK IQYTCFPNEE GGIVDDLLVY CYEPEKYLLV VNAANIEKDW
NWCVSHNTEG AELENSSDNM AQLAVQGPKA ILALQKLTDI DLSAIPYYTF TVGRFAGKEN
VIISNTGYTG AGGFELYFYP DAAEAIWKAV FEAGEEFGIK PVGLGARDTL RLEMGFCLYG
NDLDDKTSPI EAGLGWITKF VEGKEFINRP MLEKQKSEGT TRKLVGFEMI DRGIPRHGYE
LVNEEGEGIG VVTSGTMSPT RKIGIGMGYV KPEYAKVGTE ICIDMRGRKL KAIVVKPPFR
K