ID   GCSPA_PYRHO             Reviewed;         449 AA.
AC   O57708;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 45.
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=PH1995;
OS   Pyrococcus horikoshii.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=53953;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT3;
RX   MEDLINE=98344137; PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y.,
RA   Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y.,
RA   Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K.,
RA   Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA31122.1; -; Genomic_DNA.
DR   PIR; C71216; C71216.
DR   RefSeq; NP_143817.1; -.
DR   GeneID; 1442838; -.
DR   GenomeReviews; BA000001_GR; PH1995.
DR   KEGG; pho:PH1995; -.
DR   NMPDR; fig|70601.1.peg.1952; -.
DR   HOGENOM; O57708; -.
DR   OMA; O57708; VANASMY.
DR   BRENDA; 1.4.4.2; 74679.
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    449       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_0000166986.
SQ   SEQUENCE   449 AA;  50357 MW;  C7DE610E8A0254DC CRC64;
     MGNHYIPNSA HKEEMLKEIG LSSIEELFAD IPEKFIKEEL NLPEGKSEYE VFLEMNEILE
     KNKTVLEMPT FLGAGTYFHY IPAHVKHLIE RSEFLTSYTP YQPEISQGML QALFEYQSLI
     AELVGLPVVN SSMYDWGTAM AEAALMTVRL HKGKRKKFVV PKHTHPERLQ VLRTYTRGPE
     VEIVTVNWNE RGQVDVEDLK EKVKDAAGVY IEIPNFFGLL EEEIREVGEI AHEAGAYFVV
     GVDPTILGIV EAPGELGADI VVGEASYFGN PMNFGGPRAG IFAVKNDMKL IRQMPGRIIG
     MTKDAEGKRA FVMTLQTREQ HIRRAKATSN ICSNEALVAV AAAIHIASLG PKGIRELGEV
     ILKNTAYLKK RLSEVAEIPF DGVNFKDVLV RFDKPYREIH EELLKRNIHG GYYVGSHFPE
     LGEAALFAAT ETTRKEWVDA LISALKEVI
//