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Database: UniProt
Entry: M5E2M4_9FIRM
LinkDB: M5E2M4_9FIRM
Original site: M5E2M4_9FIRM 
ID   M5E2M4_9FIRM            Unreviewed;       445 AA.
AC   M5E2M4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE            EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
GN   Name=gcvPA {ECO:0000256|HAMAP-Rule:MF_00712};
GN   ORFNames=HSACCH_01687 {ECO:0000313|EMBL:CCU79899.1};
OS   Halanaerobium saccharolyticum subsp. saccharolyticum DSM 6643.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=1293054 {ECO:0000313|EMBL:CCU79899.1, ECO:0000313|Proteomes:UP000012063};
RN   [1] {ECO:0000313|Proteomes:UP000012063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6643 {ECO:0000313|Proteomes:UP000012063};
RX   PubMed=23640197; DOI=10.1128/genomea.00187-13;
RA   Kivisto A., Larjo A., Ciranna A., Santala V., Roos C., Karp M.;
RT   "Genome Sequence of Halanaerobium saccharolyticum subsp. saccharolyticum
RT   Strain DSM 6643T, a Halophilic Hydrogen-Producing Bacterium.";
RL   Genome Announc. 1:217-225(2013).
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:0000256|ARBA:ARBA00003788, ECO:0000256|HAMAP-
CC       Rule:MF_00712}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00043839, ECO:0000256|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:0000256|HAMAP-Rule:MF_00712}.
CC   -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00712}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCU79899.1}.
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DR   EMBL; CAUI01000021; CCU79899.1; -; Genomic_DNA.
DR   RefSeq; WP_005489202.1; NZ_CAUI01000021.1.
DR   AlphaFoldDB; M5E2M4; -.
DR   STRING; 1293054.HSACCH_01687; -.
DR   eggNOG; COG0403; Bacteria.
DR   InParanoid; M5E2M4; -.
DR   OrthoDB; 9771867at2; -.
DR   Proteomes; UP000012063; Unassembled WGS sequence.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00712; GcvPA; 1.
DR   InterPro; IPR023010; GcvPA.
DR   InterPro; IPR049315; GDC-P_N.
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; GLYCINE CLEAVAGE SYSTEM P-PROTEIN; 1.
DR   PANTHER; PTHR42806:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   PIRSF; PIRSF006815; GcvPA; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00712}; Reference proteome {ECO:0000313|Proteomes:UP000012063}.
FT   DOMAIN          2..441
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
SQ   SEQUENCE   445 AA;  49485 MW;  F61E809A8886ABB9 CRC64;
     MDYISNTAAE RNKMLKEIGI KEVEDLFSMI PEAVKADDEL NIEAGISELE LMRKAQNIAK
     KNKSLDQQIS FLGAGAYDHY VPGVIDALIS RSEFYTAYTP YQAELSQGTL EAIYEYQSMI
     SDLTGMGITN ASMLDGASAA AEAVTMGARI SRRSKVLLPD TINPSYREVI KTYGSGAELE
     FIDLESKANI IEPELIKENI DEKTAVVVLQ YPNFYGSIEK MEEISKITKG NKNIIFVVIV
     NPILLGVLKA PAEFDADIVV GEAQNLGSGL NYGGPNLGFM ACRDNRKMMR QLPGRIVGKT
     TDIEGKEGFV LTLQTREQHI RREKATSNIC TNEALNALMA TIYLSTMGKT GLKEVGEQCY
     HKAHYLAKKI DKISGFEVAN KDNFFHEFVV KTKEKSSQII DKLLQKDILV GYDLKRIDED
     GILVCVTEKR TKAEMDNLLE NLEVL
//
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