ID A0A1Y0GBR4_9PROT Unreviewed; 484 AA.
AC A0A1Y0GBR4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=CAP31_14265 {ECO:0000313|EMBL:ARU32723.1};
OS Sulfuriferula sp. AH1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sulfuricellaceae; Sulfuriferula.
OX NCBI_TaxID=1985873 {ECO:0000313|EMBL:ARU32723.1, ECO:0000313|Proteomes:UP000195558};
RN [1] {ECO:0000313|EMBL:ARU32723.1, ECO:0000313|Proteomes:UP000195558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH1 {ECO:0000313|EMBL:ARU32723.1,
RC ECO:0000313|Proteomes:UP000195558};
RA Jones D.S., Hua A.A., Roepke E.W., Bailey J.V.;
RT "The complete genome sequence of Sulfuriferula sp. str. AH1, a sulfur-
RT oxidizing autotroph isolated from weathered sulfide-bearing rock from the
RT Duluth Complex.";
RL Submitted (MAY-2017) 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: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|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: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; CP021138; ARU32723.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0GBR4; -.
DR KEGG; sulf:CAP31_14265; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000195558; 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 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 {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00713};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00713}; Reference proteome {ECO:0000313|Proteomes:UP000195558}.
FT DOMAIN 152..271
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 346..447
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 264
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00713"
SQ SEQUENCE 484 AA; 52648 MW; EFBF1EF47B95795A CRC64;
MLIFEHSRPH RAAHAQMPAH AADISDLPAS LLRQDEPLLP QASEMDVVRH YTRLSQKNFS
IDTQFYPLGS CTMKYNPRAC NSLAMLPGFL ARHPFAPATT GQGFLASMYE LQEMLKDVTG
MAGVSLAPMA GAQGEFAGVA MIRAYHDARG DDARREIIVP NAAHGTNPAT AVMCGYTVRE
IPTDKEGDVD LEALQAAVGP HTAGLMLTNP STLGVFEKKI QQIQKIVHDA GGLLYYDGAN
LNAILGRVKP GDMGFDVIHM NLHKTFSTPH GGGGPGAGPV GVAARLLPYM PVPVVTRENG
QYRLLVEGDI PATIGRMSAN HGNAGVLLRA YIYARMLGAE GMHRVAEFAT LNANYLLAEL
QKAGFDIAFP TRRASHEFIV TLKKLKDETG VTAMDFAKRL LDYGYHAPTT YFPMLVPECL
LIEPTETESR ETLDAFVAAM KTILAEAYAT PELVRGAPYT QPVRRLDDVK AARELDLVWR
QPAA
//
