ID   GCSPA_PARUW             Reviewed;         446 AA.
AC   Q6MEJ2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 32.
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=pc0283;
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiae; Chlamydiales; Parachlamydiaceae;
OC   Candidatus Protochlamydia.
OX   NCBI_TaxID=264201;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D.,
RA   Rattei T., Mewes H.-W., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(2004).
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; BX908798; CAF23007.1; -; Genomic_DNA.
DR   RefSeq; YP_007282.1; -.
DR   GeneID; 2780941; -.
DR   GenomeReviews; BX908798_GR; pc0283.
DR   KEGG; pcu:pc0283; -.
DR   NMPDR; fig|264201.1.peg.283; -.
DR   HOGENOM; Q6MEJ2; -.
DR   OMA; Q6MEJ2; VANASMY.
DR   BioCyc; CPRO264201:PC0283-MON; -.
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    446       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_1000045673.
SQ   SEQUENCE   446 AA;  49350 MW;  2C14E46369B97FDD CRC64;
     MDFISNKTPQ IEAMLTEIGI QNVEELFKSI PSSLILQAPS VDDGLSEYEG IQLIESLAVR
     NTFPNLVSYL GAGAYEHHIP ALVGAVCSKS EFLTAYTPYQ AEASQGMLQI IFEFQSAICA
     LTGMDVANAS VYDGASACAE AILMSLRHHK TRRQILLSDS LHPHYKKVIE QYLKSQDCEL
     ITVPFLQEGT LDASFLKMYL NDQTAAILLQ SPNFFGCIED VQPITEMAKS QGALTILCAN
     PISYGLLSSA KELGVDIAVG DCQPFGLSLS FGGPYAGYMA CKQELMRQLP GRIVGETLDV
     QGSRGFVLTL QAREQHIRRE KATSNICTNQ ALAALASLVA MLWYGKEGVK ELALTNYQRA
     NYLKFHLGKI STINVWNQGA SFNEFVVDFK QDSNQVLEFF RLNGIEPGIE LKRYYPSLKT
     CLLIAVTETK NQIQLDQFIK VCKELF
//