ID   B8FT30_DESHD            Unreviewed;       487 AA.
AC   B8FT30;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE            EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine cleavage system P-protein subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine decarboxylase subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
GN   Name=gcvPB {ECO:0000256|HAMAP-Rule:MF_00713};
GN   OrderedLocusNames=Dhaf_4036 {ECO:0000313|EMBL:ACL22046.1};
OS   Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL22046.1, ECO:0000313|Proteomes:UP000007726};
RN   [1] {ECO:0000313|EMBL:ACL22046.1, ECO:0000313|Proteomes:UP000007726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10664 / DCB-2 {ECO:0000313|Proteomes:UP000007726};
RX   PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA   Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA   Tiedje J.M.;
RT   "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT   anaerobe capable of dehalogenation and metal reduction.";
RL   BMC Microbiol. 12:21-21(2012).
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_00713}.
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_00713};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP-
CC         Rule:MF_00713};
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_00713}.
CC   -!- SIMILARITY: Belongs to the GcvP family. C-terminal subunit subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00713}.
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DR   EMBL; CP001336; ACL22046.1; -; Genomic_DNA.
DR   RefSeq; WP_015944974.1; NC_011830.1.
DR   AlphaFoldDB; B8FT30; -.
DR   KEGG; dhd:Dhaf_4036; -.
DR   HOGENOM; CLU_004620_5_0_9; -.
DR   Proteomes; UP000007726; 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   CDD; cd00613; GDC-P; 1.
DR   Gene3D; 6.20.440.10; -; 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_00713; GcvPB; 1.
DR   InterPro; IPR023012; GcvPB.
DR   InterPro; IPR049316; GDC-P_C.
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; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 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_00713}; Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00713}.
FT   DOMAIN          32..294
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          352..457
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   MOD_RES         272
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00713"
SQ   SEQUENCE   487 AA;  53961 MW;  B946D5E95465B448 CRC64;
     MRALEPLIFE LSREGRTGVS LPSCDVPEIP LEDLIPQEFL RDKEPELPEV SEVDVVRHFT
     RLSSFNHGVD TGFYPLGSCT MKYNPKVNEK LARLPGFSQI HPYQPEELTQ GALGLMVELQ
     EELAEITGMD AFTLQPAAGA HGEMTGILII KAYHDHRQDV KRRKVIVPDS AHGTNPATGA
     MAGYDIVQVP SNERGGVDIE ALRQVANDEV AALMLTNPNT LGLFDENILE IAEIIHSVGG
     LIYYDGANAN AIMGIARPGD MGFDVVHLNL HKTFSTPHGG GGPGSGPVGV KEFLAPYLPK
     PVAIRTPEGR YSWDEDRPLS IGRVRAFQAN FGVLVKAYAY IRALGGEGLK AASQNAVLNA
     NFLMSILKEH YHLPYDRVCM HEFIITPKNL KNYGIHTLDI AKRLLDYGYH PPTIYFPLIV
     EEAMMIEPTE TESLETLEQF ARVMIQIAEE VKQDAEMVKN APHDTLVTRL DETGAARKPD
     LRWRKPQ
//