ID   GCSPA_MOOTA             Reviewed;         444 AA.
AC   Q2RH48;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=Moth_1943;
OS   Moorella thermoacetica (strain ATCC 39073).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteriaceae; Moorella group; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f.
RT   Clostridium thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC20241.1; -; Genomic_DNA.
DR   RefSeq; YP_430784.1; -.
DR   GeneID; 3832435; -.
DR   GenomeReviews; CP000232_GR; Moth_1943.
DR   KEGG; mta:Moth_1943; -.
DR   NMPDR; fig|264732.9.peg.1952; -.
DR   HOGENOM; Q2RH48; -.
DR   OMA; Q2RH48; VANASMY.
DR   BioCyc; MTHE264732:MOTH_1943-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    444       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_1000045669.
SQ   SEQUENCE   444 AA;  48030 MW;  8508D45D24DE1705 CRC64;
     MTYIPTTAAE QQQMLAACGA HRMEELFSDV PASVRLGREL NLPRPMAEAE VWRHLEELAG
     KNKKLVSFLG AGAYEHYIPS VVGHLLARSE FYTAYTPYQP EISQGTLQAI FEFQSLICEL
     TGLDVATASH YDGATAMAEA ALVACNATRR QKILVSRSVN PQYRTVLSTY AKGQGVELAE
     VPLQDGRTDL EALEKLAGKD VAGVILQNPN FFGQIEAMAE ATDLAHKARA LGIAVVDPVS
     LGLLAAPGEY GADLAVGEGQ SLGNPLNFGG PYLGFIAARE KLVRRLPGRI VGQTKDVDGK
     RAYVLTLQAR EQHIRREKAT SNICSNEALC ALAATIYLAA MGREGLKEVA SQCLLKAHYA
     QKKLAALPGV TPVFNGPFFH EFVLQTKLSP ATVARRLAEN GFAAGFDLGR FYPELKNALL
     FTVTEVRTRE EIDALVAAMR GILA
//