ID   GCSPA_CAUCR             Reviewed;         448 AA.
AC   Q9A353;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JUN-2009, entry version 39.
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=CC_3353;
OS   Caulobacter crescentus (Caulobacter vibrioides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=155892;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   MEDLINE=21173698; PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J.,
RA   Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J.,
RA   Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L.,
RA   Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK25315.1; -; Genomic_DNA.
DR   PIR; G87664; G87664.
DR   RefSeq; NP_422147.1; -.
DR   GeneID; 943794; -.
DR   GenomeReviews; AE005673_GR; CC_3353.
DR   KEGG; ccr:CC_3353; -.
DR   NMPDR; fig|190650.1.peg.3327; -.
DR   TIGR; CC_3353; -.
DR   HOGENOM; Q9A353; -.
DR   OMA; Q9A353; VANASMY.
DR   BRENDA; 1.4.4.2; 2191.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) act...; IEA:EC.
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    448       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_0000166962.
SQ   SEQUENCE   448 AA;  47298 MW;  D62740DA0E84303F CRC64;
     MRYLPLTPED RVEMLGAIGV KSIDDLFVDV PVSARRDAPV DLPHHAGELD VEREMAGLAR
     RNRAAGEGPF FCGAGAYRHH VPATVDHIIQ RSEFLTSYTP YQPEIAQGTL QVLFEFQTQV
     AALTGMEVAN ASLYDGSTGA AEAVMMAQRV TRRNKAVMSG GVHPHYVGAI ETLAHAAGVA
     TQALPAAVDA EDAVIAAIDQ DTACVVVQTP NVFGTVTDVS KIAEAAHAAG ALLIVVTTEA
     VSFGLLKSPG EMGADIAVAE GQSIGNGLNF GGPYVGLFAC KEKFVRQMPG RLCGETVDAD
     GKRGFVLTLS TREQHIRRDK ATSNICTNSG LCALAFSIHM SLLGETGLRQ LAAVNHQKAL
     ALRDALKAVP GVEILTPRFF NEFAIRVPGK AAEVVEILAA HGVIAGVPFS RLDAKAGLDD
     VLLVAATETT LDIDIPVFAK ALTKVFAQ
//