GCST_BACSU
ID GCST_BACSU Reviewed; 362 AA.
AC P54378;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 140.
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}; Synonyms=yqhI;
GN OrderedLocusNames=BSU24570;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 236-237.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D84432; BAA12546.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14388.2; -; Genomic_DNA.
DR PIR; H69958; H69958.
DR RefSeq; NP_390337.2; NC_000964.3.
DR RefSeq; WP_004398598.1; NZ_JNCM01000036.1.
DR PDB; 1YX2; X-ray; 2.08 A; A/B=1-362.
DR PDBsum; 1YX2; -.
DR AlphaFoldDB; P54378; -.
DR SMR; P54378; -.
DR STRING; 224308.BSU24570; -.
DR jPOST; P54378; -.
DR PaxDb; P54378; -.
DR PRIDE; P54378; -.
DR EnsemblBacteria; CAB14388; CAB14388; BSU_24570.
DR GeneID; 938547; -.
DR KEGG; bsu:BSU24570; -.
DR PATRIC; fig|224308.179.peg.2675; -.
DR eggNOG; COG0404; Bacteria.
DR InParanoid; P54378; -.
DR OMA; MPVQYPA; -.
DR PhylomeDB; P54378; -.
DR BioCyc; BSUB:BSU24570-MON; -.
DR EvolutionaryTrace; P54378; -.
DR Proteomes; UP000001570; 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..362
FT /note="Aminomethyltransferase"
FT /id="PRO_0000122543"
FT CONFLICT 236..237
FT /note="KL -> NV (in Ref. 1; BAA12546)"
FT /evidence="ECO:0000305"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 94..104
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:1YX2"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 189..200
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:1YX2"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1YX2"
FT TURN 250..254
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 282..293
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 307..318
FT /evidence="ECO:0007829|PDB:1YX2"
FT TURN 319..322
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 323..331
FT /evidence="ECO:0007829|PDB:1YX2"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:1YX2"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:1YX2"
SQ SEQUENCE 362 AA; 39807 MW; 25D814C97FE94A1B CRC64;
MLKRTPLFDL YKEYGGKTID FGGWELPVQF SSIKKEHEAV RTAAGLFDVS HMGEVEVSGN
DSLSFLQRLM TNDVSALTPG RAQYTAMCYP DGGTVDDLLI YQKGENRYLL VINASNIDKD
LAWMKEHAAG DVQIDNQSDQ IALLAVQGPK AEAILKNLTD ADVSALKPFA FIDEADISGR
KALISRTGYT GEDGYEIYCR SDDAMHIWKK IIDAGDAYGL IPCGLGARDT LRFEAKLPLY
GQELTRDITP IEAGIGFAVK HKKESDFFGK SVLSEQKENG AKRKLVGLEM IEKGIPRHGY
EVFQNGKSVG KVTTGTQSPT LGKNVGLALI DSETSEIGTV VDVEIRKKLV KAKVVKTPFY
KR
