(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 131.
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}.
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   SMR; P54378; -.
DR   STRING; 224308.BSU24570; -.
DR   jPOST; P54378; -.
DR   PaxDb; P54378; -.
DR   PRIDE; P54378; -.
DR   EnsemblBacteria; CAB14388; CAB14388; BSU24570.
DR   GeneID; 938547; -.
DR   KEGG; bsu:BSU24570; -.
DR   PATRIC; fig|224308.179.peg.2675; -.
DR   eggNOG; ENOG4105D43; Bacteria.
DR   eggNOG; COG0404; LUCA.
DR   HOGENOM; HOG000239381; -.
DR   InParanoid; P54378; -.
DR   KO; K00605; -.
DR   OMA; MPVQYPA; -.
DR   PhylomeDB; P54378; -.
DR   BioCyc; BSUB:BSU24570-MONOMER; -.
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   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   PIRSF; PIRSF006487; GcvT; 1.
DR   SUPFAM; SSF101790; SSF101790; 1.
DR   TIGRFAMs; TIGR00528; gcvT; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P54378.
DR   SWISS-2DPAGE; P54378.
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:0000244|PDB:1YX2"
FT   HELIX           11..14
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          17..21
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          24..31
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   HELIX           33..42
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          43..48
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          52..59
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   HELIX           62..69
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          70..72
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   HELIX           74..76
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          81..88
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          94..104
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          107..112
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   HELIX           114..116
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   HELIX           117..126
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          133..136
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   TURN            138..140
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          141..148
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   HELIX           151..156
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          159..161
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   HELIX           163..165
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          170..177
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          180..186
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          189..200
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   HELIX           201..203
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   HELIX           204..215
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   HELIX           216..218
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          220..223
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   HELIX           225..234
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   TURN            240..242
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          243..245
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   TURN            250..254
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   HELIX           256..258
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   HELIX           270..279
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          282..293
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          301..304
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          307..318
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   TURN            319..322
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          323..331
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   HELIX           332..334
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          340..345
FT                   /evidence="ECO:0000244|PDB:1YX2"
FT   STRAND          348..355
FT                   /evidence="ECO:0000244|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
//

If you have problems or comments...

PBIL Back to PBIL home page