ID   GCSPA_HYPNA             Reviewed;         447 AA.
AC   Q0BYP2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-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=HNE_2721;
OS   Hyphomonas neptunium (strain ATCC 15444).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=228405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980487; DOI=10.1128/JB.00111-06;
RA   Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T.,
RA   Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E.,
RA   Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A.,
RA   Rosovitz M.J., Madupu R., Brinkac L.M., Durkin A.S., Daugherty S.C.,
RA   Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D.,
RA   Davidsen T.M., Yang Q., Zafar N., Ward N.L.;
RT   "Comparative genomic evidence for a close relationship between the
RT   dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT   crescentus.";
RL   J. Bacteriol. 188:6841-6850(2006).
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; CP000158; ABI76120.1; -; Genomic_DNA.
DR   RefSeq; YP_761401.1; -.
DR   GeneID; 4288474; -.
DR   GenomeReviews; CP000158_GR; HNE_2721.
DR   KEGG; hne:HNE_2721; -.
DR   NMPDR; fig|228405.5.peg.2608; -.
DR   TIGR; HNE_2721; -.
DR   HOGENOM; Q0BYP2; -.
DR   OMA; Q0BYP2; VANASMY.
DR   BioCyc; HNEP81032:HNE_2721-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    447       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_1000045659.
SQ   SEQUENCE   447 AA;  46985 MW;  E724A1B01F97A95B CRC64;
     MRYLPLTPED RANMLATIGA KSVDDFYTDV PDAARLKGKI AGLPDHQGEL AVERHLTKLA
     AKNRSASSGP FFVGAGAYKH HVPATVDMII QRSEFLTTYT PYQPEIAQGT LQTLFEFQTQ
     VASLTAMDVA NASMYDGSTS CAEAAVMAAR VTRRKKIILS GGLHPHYAAA TRLLAEAQGL
     TVVQLPVAID GEGELAKAVD GETACVIGQS PNVFGTVTDL SAVADAAHGK GALLVSVFTE
     AVSLGLVTPP GEMGADIAAG EGQSIGNGLN FGGPYVGLFS CREKLVRQMP GRLCGETVDA
     DGKRGFVLTL STREQHIRRD KATSNICTNS GLCALAFTSH MTLLGGKGLK QLAELNHEAA
     IELADALGAV KGVEILTPRF FNEFAIRTPM DAEAVLAMLD EAGVVGGVRA SRLFPGDHLG
     DVILVAATEC TTADDIAAYT DALKEII
//