ID   GCSPA_MARSD             Reviewed;         443 AA.
AC   C6C0V0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
GN   Name=gcvPA {ECO:0000255|HAMAP-Rule:MF_00712}; OrderedLocusNames=Desal_2995;
OS   Maridesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIMB 8403 /
OS   VKM B-1763) (Desulfovibrio salexigens).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Maridesulfovibrio.
OX   NCBI_TaxID=526222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14822 / DSM 2638 / NCIMB 8403 / VKM B-1763;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio salexigens DSM 2638.";
RL   Submitted (JUN-2009) 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 through
CC       its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC       methylamine moiety is then transferred to the lipoamide cofactor of the
CC       H protein. {ECO:0000255|HAMAP-Rule:MF_00712}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC         glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC         [glycine-cleavage complex H protein] + CO2; Xref=Rhea:RHEA:24304,
CC         Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83143; EC=1.4.4.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00712};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. In this organism, the P 'protein' is a heterodimer of two
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00712}.
CC   -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00712}.
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DR   EMBL; CP001649; ACS81047.1; -; Genomic_DNA.
DR   RefSeq; WP_015852863.1; NC_012881.1.
DR   AlphaFoldDB; C6C0V0; -.
DR   SMR; C6C0V0; -.
DR   STRING; 526222.Desal_2995; -.
DR   EnsemblBacteria; ACS81047; ACS81047; Desal_2995.
DR   KEGG; dsa:Desal_2995; -.
DR   eggNOG; COG0403; Bacteria.
DR   HOGENOM; CLU_004620_0_2_7; -.
DR   OMA; MYDGASA; -.
DR   OrthoDB; 870147at2; -.
DR   Proteomes; UP000002601; Chromosome.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   CDD; cd00613; GDC-P; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00712; GcvPA; 1.
DR   InterPro; IPR023010; GcvPA.
DR   InterPro; IPR020581; GDC_P.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR42806; PTHR42806; 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   PIRSF; PIRSF006815; GcvPA; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..443
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 1"
FT                   /id="PRO_1000212659"
SQ   SEQUENCE   443 AA;  48716 MW;  998A3B75AB2E2299 CRC64;
     MPYVPHSPEE IREMLDVIGV NSVEDLFAEI PAELRPKSFN LPKGKSEMAV LQQLDKMAAK
     NTTDLTSFLG AGFYDHFIPT AVDALSSRSE FYTAYTPYQP ESSQGTLQAI FEYQTAMARL
     MDMDYANASV YDGGSALYEA TLMAVRKTRR RKIIVSEALN PIYRVMLDSY TTNLNLELVT
     VPHNHGRTNV KSITAAVDKD TAAVIVQNPN FFGSVNDFTE MFAAVHEHKA LAIMSTYPVM
     QSVLKTPGQM GADIAVADGQ SIGQPLSFGG PYLGIMTCSK ALVRQMPGRI AGRTEDEDGK
     TGYVLTIQAR EQHIRRQKAT SNICSNQALC ALRTLIHLCL LGEEGLNRTA VLSVERAHYA
     AERLTAIDGV EMFTKGPFGN EFAVTLPVNA FEVIDKLTER GIIPGFPVGR YYEGLENVLL
     VACTEKTTEE QIGIFAEILR GTI