GCST_THEMA
ID GCST_THEMA Reviewed; 364 AA.
AC Q9WY54;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=TM_0211;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD35303.1; -; Genomic_DNA.
DR PIR; E72403; E72403.
DR RefSeq; NP_228026.1; NC_000853.1.
DR RefSeq; WP_004082884.1; NZ_CP011107.1.
DR PDB; 1WOO; X-ray; 2.40 A; A=1-364.
DR PDB; 1WOP; X-ray; 2.00 A; A=1-364.
DR PDB; 1WOR; X-ray; 1.95 A; A=1-364.
DR PDB; 1WOS; X-ray; 1.84 A; A=1-364.
DR PDBsum; 1WOO; -.
DR PDBsum; 1WOP; -.
DR PDBsum; 1WOR; -.
DR PDBsum; 1WOS; -.
DR AlphaFoldDB; Q9WY54; -.
DR SMR; Q9WY54; -.
DR STRING; 243274.THEMA_03670; -.
DR DrugBank; DB03256; (6R)-Folinic acid.
DR DrugBank; DB03760; Dihydrolipoic Acid.
DR EnsemblBacteria; AAD35303; AAD35303; TM_0211.
DR KEGG; tma:TM0211; -.
DR eggNOG; COG0404; Bacteria.
DR InParanoid; Q9WY54; -.
DR OMA; MPVQYPA; -.
DR OrthoDB; 282830at2; -.
DR BRENDA; 1.4.1.27; 6331.
DR EvolutionaryTrace; Q9WY54; -.
DR Proteomes; UP000008183; 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 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Reference proteome; Transferase.
FT CHAIN 1..364
FT /note="Aminomethyltransferase"
FT /id="PRO_0000122610"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:1WOS"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:1WOS"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1WOS"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1WOS"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:1WOS"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1WOS"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:1WOS"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1WOS"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1WOP"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 188..199
FT /evidence="ECO:0007829|PDB:1WOS"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:1WOS"
FT HELIX 203..217
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1WOO"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:1WOS"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:1WOS"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:1WOS"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1WOS"
FT HELIX 267..275
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 279..289
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 303..314
FT /evidence="ECO:0007829|PDB:1WOS"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:1WOS"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:1WOS"
FT STRAND 344..351
FT /evidence="ECO:0007829|PDB:1WOS"
SQ SEQUENCE 364 AA; 40333 MW; 66F33CCC151CC6F1 CRC64;
MKRTPLFEKH VELGAKMVDF AGWEMPLYYT SIFEEVMAVR KSVGMFDVSH MGEFLVKGPE
AVSFIDFLIT NDFSSLPDGK AIYSVMCNEN GGIIDDLVVY KVSPDEALMV VNAANIEKDF
NWIKSHSKNF DVEVSNISDT TALIAFQGPK AQETLQELVE DGLEEIAYYS FRKSIVAGVE
TLVSRTGYTG EDGFELMLEA KNAPKVWDAL MNLLRKIDGR PAGLGARDVC RLEATYLLYG
QDMDENTNPF EVGLSWVVKL NKDFVGKEAL LKAKEKVERK LVALELSGKR IARKGYEVLK
NGERVGEITS GNFSPTLGKS IALALVSKSV KIGDQLGVVF PGGKLVEALV VKKPFYRGSV
RREV
