GCST_PARD8
ID GCST_PARD8 Reviewed; 361 AA.
AC A6L8T3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=BDI_0312;
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR42097.1; -; Genomic_DNA.
DR RefSeq; WP_011965962.1; NC_009615.1.
DR AlphaFoldDB; A6L8T3; -.
DR SMR; A6L8T3; -.
DR STRING; 435591.BDI_0312; -.
DR EnsemblBacteria; ABR42097; ABR42097; BDI_0312.
DR KEGG; pdi:BDI_0312; -.
DR PATRIC; fig|435591.13.peg.307; -.
DR eggNOG; COG0404; Bacteria.
DR HOGENOM; CLU_007884_10_2_10; -.
DR OMA; MPVQYPA; -.
DR OrthoDB; 282830at2; -.
DR BioCyc; PDIS435591:G1G5A-322-MON; -.
DR Proteomes; UP000000566; 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; Reference proteome; Transferase.
FT CHAIN 1..361
FT /note="Aminomethyltransferase"
FT /id="PRO_1000047684"
SQ SEQUENCE 361 AA; 39544 MW; 1D729D0400519CD5 CRC64;
MKTTPFTDVH IALGAKMHEF AGFNMPIEYS GIIDEHMTVV NGVGVFDVSH MGEFWVKGPN
ALAFIQSVTS NDASVLPLGK AQYTCFPNDK GGIVDDLLVY HYEPEKYLLV VNAGNIDKDW
EWCVSHNTVG AELENSSDRT AQLAIQGPKA QEVLQRLTPV DLSSIPYYSF VTGEFAGCKN
VIISNTGYTG AGGFELYFYP SDGMTIWNAI FEAGKPEGIK PIGLGARDTL RLEMGFCLYG
NDLDDTTSPI EAGLGWITKF AEGKNFTNRA ELERQKKEGV TRKLCAFELQ EKGIPRHGYE
IADAEGNVIG VVTSGTMSPV LKKGIGMGYV KPEFAKAGTD IFIKVRNKNL KAQVVKAPFR
K