(data stored in SCRATCH zone)

SWISSPROT: GCSPA_BACSU

ID   GCSPA_BACSU             Reviewed;         448 AA.
AC   P54376;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   11-DEC-2019, entry version 122.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1;
DE            EC=1.4.4.2;
DE   AltName: Full=Glycine cleavage system P-protein subunit 1;
DE   AltName: Full=Glycine decarboxylase subunit 1;
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1;
GN   Name=gcvPA; Synonyms=yqhJ; OrderedLocusNames=BSU24560;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
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 265-266.
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. The P protein binds the alpha-amino group of glycine through
CC       its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC       methylamine moiety is then transferred to the lipoamide cofactor of the
CC       H protein (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + N(6)-lipoyl-L-lysyl-[glycine-cleavage complex
CC         H protein] = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC         [glycine-cleavage complex H protein] + CO2; Xref=Rhea:RHEA:24304,
CC         Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83143; EC=1.4.4.2;
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. In this organism, the P 'protein' is a heterodimer of two
CC       subunits.
CC   -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC       {ECO:0000305}.
DR   EMBL; D84432; BAA12547.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14387.2; -; Genomic_DNA.
DR   PIR; A69959; A69959.
DR   RefSeq; NP_390336.2; NC_000964.3.
DR   RefSeq; WP_003230207.1; NZ_JNCM01000036.1.
DR   SMR; P54376; -.
DR   STRING; 224308.BSU24560; -.
DR   PaxDb; P54376; -.
DR   PRIDE; P54376; -.
DR   EnsemblBacteria; CAB14387; CAB14387; BSU24560.
DR   GeneID; 938546; -.
DR   KEGG; bsu:BSU24560; -.
DR   PATRIC; fig|224308.179.peg.2674; -.
DR   eggNOG; ENOG4107QK8; Bacteria.
DR   eggNOG; COG0403; LUCA.
DR   HOGENOM; HOG000132025; -.
DR   InParanoid; P54376; -.
DR   KO; K00282; -.
DR   OMA; MYDGASA; -.
DR   PhylomeDB; P54376; -.
DR   BioCyc; BSUB:BSU24560-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   CDD; cd00613; GDC-P; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00712; GcvPA; 1.
DR   InterPro; IPR023010; GcvPA.
DR   InterPro; IPR020581; GDC_P.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR42806; PTHR42806; 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   PIRSF; PIRSF006815; GcvPA; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
DR   PRODOM; P54376.
DR   SWISS-2DPAGE; P54376.
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..448
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 1"
FT                   /id="PRO_0000166961"
FT   CONFLICT        265..266
FT                   /note="QP -> HR (in Ref. 1; BAA12547)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   448 AA;  49429 MW;  441875530A324E3F CRC64;
     MKHRYLPATE KDKQEMLATI GVSSIDDLFA DIPENVKYKK EHQIKKAKSE TELTRELTKL
     ASKNRDTVQY ASFLGAGVYD HYQPVIVDHV ISRSEFYTAY TPYQPEISQG ELQAIFEFQT
     MICELTGMDI ANSSMYDGGT ALAEAAMLAS GHTKKKKIVV SKTVHPESRE VLKTYAKGQY
     IDVVEVPAAD GVTDLDALRQ TVCENTAAVI VQYPNFFGRI EPLKDIEPIA HQGKSMFIVS
     ANPLALGLLT PPGKFQSDIV VGDAQPFGIP SAYGGPHCGF FAVTKKLMRK VPGRLVGQTE
     DENGKRGFVL TLQAREQHIR RDKATSNICS NQALNALAAS VAMTALGKNG VKDIARQNLL
     KANYAKQEAK KAGLTVMFDG PMFNEFVIKL DEPVRAVNKR LLAKGMIGGY DLGLTYPELD
     CHMLIAVTEL RTKEEIDALI QELGDRHE
//

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