ID   GCSPA_FRATH             Reviewed;         455 AA.
AC   Q2A4V1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=FTL_0479;
OS   Francisella tularensis subsp. holarctica (strain LVS).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=376619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S.,
RA   Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R.,
RA   Garcia E.;
RT   "Complete genome sequence of Francisella tularensis LVS (Live Vaccine
RT   Strain).";
RL   Submitted (MAR-2006) 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; AM233362; CAJ78919.1; -; Genomic_DNA.
DR   RefSeq; YP_513251.1; -.
DR   GeneID; 3952537; -.
DR   GenomeReviews; AM233362_GR; FTL_0479.
DR   KEGG; ftl:FTL_0479; -.
DR   HOGENOM; Q2A4V1; -.
DR   OMA; Q2A4V1; VANASMY.
DR   BioCyc; FTUL351581:FTL_0479-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    455       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_1000045651.
SQ   SEQUENCE   455 AA;  49667 MW;  02B10BD6E9DB2715 CRC64;
     MSFIPHKLEQ IKKMLDTIGA SSVDQLFDEI PRHLRADTLN IKDGINEIQL ANLMRKRANK
     NHHNINYIGA GAYSHHIPAA IWDIVARGEF YTAYTPYQAE ASQGGLQVIY EFQTMMAGLT
     GMDASNASMY DGATALAESV LMAIRSNKKA KSQKVLIAEA LHPTYLRVLE TITKHQGIEF
     DIVNLDSKNG KTDVTKLEDF ANTNYAAVVI QSPNFLGQLA DVDGITNWAH KHGALVIAVT
     NPMSLAILKS PAEWGDNGAD IVCGEGQPIG VPLASGGPYF GFMTCKMAHV RQMPGRIVGR
     TVDLDGNEGF CLTLQAREQH IRRAKATSNI CTNQGLMVTA ATIYMSLLGA EGLERVASIS
     HENTQTLATE LAKINGVSIR FNSAFFNEVV IDLPVNAETF VTEMEKEAID AGYFLGEYHS
     DLANSIMVCA TEIHTSEDIK EYIEATKKVL ARIGG
//