ID   GCSPB_RHOBA             Reviewed;         500 AA.
AC   Q7UNH1;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine cleavage system P-protein subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine decarboxylase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
GN   Name=gcvPB {ECO:0000255|HAMAP-Rule:MF_00713};
GN   OrderedLocusNames=RB7584;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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_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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00713};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_00713}.
CC   -!- SIMILARITY: Belongs to the GcvP family. C-terminal subunit subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00713}.
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DR   EMBL; BX294146; CAD75448.1; -; Genomic_DNA.
DR   RefSeq; NP_867901.1; NC_005027.1.
DR   RefSeq; WP_011121465.1; NC_005027.1.
DR   AlphaFoldDB; Q7UNH1; -.
DR   SMR; Q7UNH1; -.
DR   STRING; 243090.RB7584; -.
DR   EnsemblBacteria; CAD75448; CAD75448; RB7584.
DR   KEGG; rba:RB7584; -.
DR   PATRIC; fig|243090.15.peg.3664; -.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_5_0_0; -.
DR   InParanoid; Q7UNH1; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR   GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
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; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR023012; GcvPB.
DR   InterPro; IPR049316; GDC-P_C.
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; PF00266; Aminotran_5; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..500
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 2"
FT                   /id="PRO_0000167010"
FT   MOD_RES         273
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00713"
SQ   SEQUENCE   500 AA;  54548 MW;  D7976005C686D1D4 CRC64;
     MRNQQSTQLL FELSRAGRRA HRLGDLDVPS VNVDELFADE ALAETPPPLP ELAEGDVVRH
     FVGLSTLNMS VDTHFYPLGS CTMKYNPKRN ERIASLPGFL NVHPLQHESG LQGLLELLYE
     LQGMFAEISG LPGVSMQPAA GAHGELAALL VAAAYFREQG SDRNVVLTAD SAHGTNPASA
     QMAGFKTKTV KSNANGLVDL EDLKAKLDDK TAVFMLTNPN TLGLFDRQIE EINKLVHDAG
     ALIYLDGANM NAILGITRPG DFGADLMHYN PHKTFSGPHG GGGPGAGPIC VRDFLAKYLP
     GPIVTRVENE NASGDDDRYT YHLTSPSDDS IGRVRSFFGN TGVLVRAYIY LRTYGGDGLR
     HVSEDAVLGA NYLLSKVKHF LDVPHGDRCM HEFVASATRL KKEKKLSAMD IAKRILDYGF
     HAPTVYFPLV VDEAVMVEPT ETESKQTLDA FVEALFRITE EGEELIHDAP HSTRISRPDD
     VTAARRPILK WTDAAGESAT
//