ID   GCSPA_CAUSK             Reviewed;         453 AA.
AC   B0T014;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-NOV-2008, entry version 8.
DE   RecName: Full=Probable glycine dehydrogenase [decarboxylating] subunit 1;
DE            EC=1.4.4.2;
DE   AltName: Full=Glycine decarboxylase subunit 1;
DE   AltName: Full=Glycine cleavage system P-protein subunit 1;
GN   Name=gcvPA; OrderedLocusNames=Caul_4384;
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=366602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S.,
RA   Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. The P protein binds the alpha-amino group of glycine
CC       through its pyridoxal phosphate cofactor; CO(2) is released and
CC       the remaining methylamine moiety is then transferred to the
CC       lipoamide cofactor of the H protein (By similarity).
CC   -!- CATALYTIC ACTIVITY: Glycine + H-protein-lipoyllysine = H-protein-
CC       S-aminomethyldihydrolipoyllysine + CO(2).
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins:
CC       P, T, L and H. In this organism, the P 'protein' is an heterodimer
CC       of two subunits (By similarity).
CC   -!- SIMILARITY: Belongs to the gcvP family. N-terminal subunit
CC       subfamily.
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DR   EMBL; CP000927; ABZ73504.1; -; Genomic_DNA.
DR   RefSeq; YP_001686002.1; -.
DR   GeneID; 5901845; -.
DR   GenomeReviews; CP000927_GR; Caul_4384.
DR   KEGG; cak:Caul_4384; -.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) act...; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavag...; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_00712; -; 1.
DR   InterPro; IPR003437; GDC-P.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   PANTHER; PTHR11773; GDC-P; 1.
DR   Pfam; PF02347; GDC-P; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Oxidoreductase.
FT   CHAIN         1    453       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_1000083218.
SQ   SEQUENCE   453 AA;  47702 MW;  F3ADFB32DA0E1647 CRC64;
     MRYLPLTPED RADMLGVIGA ETIDALFVDV PAVAYRKDPV DLPFHAGELE VEREMLALSR
     RNRSASEGPF FVGAGAYRHH VPATVDHIIQ RSEFLTSYTP YQPEIAQGTL QVLFEFQTQV
     AALTGMEVAN ASLYDGSTAT AEAVMMATRV TRRGKAVLSG GVHPHYVGTV ETLAHAAGVA
     TERLKAAIDA EDAVIAAIDA DTACVVVQTP NVFGTATDVS KIAAAAQAAG ALLIVVTTEA
     VSYGLLKSPG EMGADIVVAE GQSIGNGLNF GGPYVGLFAC KEKYVRQAPG RLCGETVDAD
     GRRGFVLTLS TREQHIRRDK ATSNICTNSG LCALAFSIHM SLLGEKGLRQ LALVNHHKAV
     KLRDALAAVP GVEVLTPRFF NEFAIKVPGN AAELVETLAA NGVIGGVPFS RLDPGAGLDN
     VLLVAATETT PDSDIALFSK ALSKVLAPKG SNQ
//