ID   GCSPA_ALCBS             Reviewed;         452 AA.
AC   Q0VLA8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
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=ABO_2592;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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; AM286690; CAL18040.1; -; Genomic_DNA.
DR   RefSeq; YP_694312.1; -.
DR   GeneID; 4211691; -.
DR   GenomeReviews; AM286690_GR; ABO_2592.
DR   KEGG; abo:ABO_2592; -.
DR   NMPDR; fig|393595.12.peg.2596; -.
DR   HOGENOM; Q0VLA8; -.
DR   OMA; Q0VLA8; VANASMY.
DR   BioCyc; ABOR393595:ABO_2592-MON; -.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) act...; IEA:EC.
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   PANTHER; PTHR11773; GDC-P; 1.
DR   Pfam; PF02347; GDC-P; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Oxidoreductase.
FT   CHAIN         1    452       Probable glycine dehydrogenase
FT                                [decarboxylating] subunit 1.
FT                                /FTId=PRO_1000045634.
SQ   SEQUENCE   452 AA;  48258 MW;  C06CE02A24606C06 CRC64;
     MPYIPHTPDD VRAMLDAIGA DSIEDLFDEI PSHLKAAGKL DALPEGLSEM DVTRLMSDRA
     AQDAGAVSFI GAGAYQHHVP AAVWEIATRG EFYTAYTPYQ AEASQGTLQV IYEFQTLMTR
     LTGMDVSNAS VYDGASGLAE AVLMSLRANR KSKSRKVLVP TAVNPRYTSA TQAIVENQDV
     ALERVGFDAA SGQTPLDALK PYEGEDYAAL VISQPNFFGS LEEVDALTDW AHANKMLVIG
     VVNPTSLALL TPPGEWGADG ADIVVGEGQP LGVPLSSGGP YFGFMCCKQK HVRQMPGRII
     GRTVDMEGKQ GFTLTLQARE QHIRRSKATS NICTNQGLAM TAATIYTSLL GPDGLGNVAA
     HCHANTQALA DKLTAIDGVE RAFTAPTFHE VVLTLPKPAD QVLAALAEKD VLGGVSLAGD
     YDMNNAILVN ATEVHSEQDL QLFEQALKEV LA
//