ID   GCSPA_CHLTE             Reviewed;         444 AA.
AC   Q8KC05;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 36.
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; Synonyms=gcvP1; OrderedLocusNames=CT1625;
OS   Chlorobium tepidum.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=1097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49652 / DSM 12025 / TLS;
RX   MEDLINE=22103685; PubMed=12093901; DOI=10.1073/pnas.132181499;
RA   Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M.,
RA   Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F.,
RA   Holt I.E., Umayam L.A., Mason T.M., Brenner M., Shea T.P.,
RA   Parksey D.S., Nierman W.C., Feldblyum T.V., Hansen C.L., Craven M.B.,
RA   Radune D., Vamathevan J.J., Khouri H.M., White O., Gruber T.M.,
RA   Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., Fraser C.M.;
RT   "The complete genome sequence of Chlorobium tepidum TLS, a
RT   photosynthetic, anaerobic, green-sulfur bacterium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM72850.1; -; Genomic_DNA.
DR   RefSeq; NP_662508.1; -.
DR   GeneID; 1006116; -.
DR   GenomeReviews; AE006470_GR; CT1625.
DR   KEGG; cte:CT1625; -.
DR   NMPDR; fig|194439.1.peg.1602; -.
DR   TIGR; CT1625; -.
DR   HOGENOM; Q8KC05; -.
DR   OMA; Q8KC05; VANASMY.
DR   BioCyc; CTEP194439:CT_1625-MON; -.
DR   BRENDA; 1.4.4.2; 189605.
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_0000166963.
SQ   SEQUENCE   444 AA;  47739 MW;  334273FF9723BB7F CRC64;
     MPFIVNTDAE RAEMLREIGV ENFEALIADI PEEIRLKKAL DLFPAMGEPE VKSLLEKMAS
     GNAATCDHVS FLGAGAYDHF IPSAVKTIAS RSEFYTAYTP YQAEVSQGTL QAIYEYQSVM
     CRLYGMDVAN ASMYDGASAL AEAALIALNV TGRNGIVVAG KLHPYTSQVL ETYLEAAGDR
     SIVQNGLENG IGSVEALEAL VSSETAAVIV QQPNFYGCLE EVEAIGEIAR KNGALFIVSA
     DPVSLGVLEA PGNYGADIAV GEGQSVGNAQ SFGGPYLGIL TVKQAHVRKI PGRLVGMTKD
     KDGNDGFILT LQTREQHIRR EKATSNICSN QALCALQSVV HLSLLGKEGI RDVANRSMQK
     AHYLADRIAE LPGYSMKFSA PFFREFVVET PVPSATIIEK MLEKKVFAGV DLSAWGEDGL
     LVAVTEKRTK EELDSFVSEL AALG
//