ID A0A1V4CYD3_9ACTN Unreviewed; 971 AA.
AC A0A1V4CYD3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000256|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000256|HAMAP-Rule:MF_00711};
GN ORFNames=VT50_0227785 {ECO:0000313|EMBL:OPF73761.1};
OS Streptomyces antioxidans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1507734 {ECO:0000313|EMBL:OPF73761.1, ECO:0000313|Proteomes:UP000033615};
RN [1] {ECO:0000313|EMBL:OPF73761.1, ECO:0000313|Proteomes:UP000033615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC164 {ECO:0000313|Proteomes:UP000033615};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces antioxidans MUSC 164.";
RL Submitted (DEC-2016) 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_00711}.
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_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00711, ECO:0000256|PIRSR:PIRSR603437-50};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|HAMAP-Rule:MF_00711}.
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:OPF73761.1}.
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DR EMBL; LAKD02000086; OPF73761.1; -; Genomic_DNA.
DR RefSeq; WP_046086992.1; NZ_LAKD02000086.1.
DR AlphaFoldDB; A0A1V4CYD3; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000033615; Unassembled WGS sequence.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR CDD; cd00613; GDC-P; 2.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR HAMAP; MF_00711; GcvP; 1.
DR InterPro; IPR003437; GcvP.
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 NCBIfam; TIGR00461; gcvP; 1.
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; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00711};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00711,
KW ECO:0000256|PIRSR:PIRSR603437-50}.
FT DOMAIN 19..448
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 462..746
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 792..913
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 719
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 971 AA; 102890 MW; 0E7B1F07044B485E CRC64;
MTANRIALSD LESGTPFERR HIGPDGEAQA KMLAQVGFGS LDELTEAAVP DVIKSTEALD
ALPSARSEPE VLAELRALAD RNQVLASMIG LGYYGTHTPP VILRNVLENP AWYTAYTPYQ
PEISQGRLEA LLNFQTVVAD LTGLPTAGSS LLDEATAAAE AMALSRRVGK VKEGVFLIDA
DCLPQTVAVI RARAEPTGVE VVVADLAEGI PDDIAERGVF GVLLQYPGAS GVVRDPRPVI
ERAHELGAVV TVAADLLALT LLTPPGELGA DIAVGSSQRF GVPMGFGGPH AGFMAVRDAY
ARNLPGRLVG VSVDADGDKA YRLALQTREQ HIRREKATSN ICTAQVLLAV MAGMYAVYHG
PDGLAAIARR THRYASVLAE GLRAGGVEVV HGAFFDTLTA RVPGRAAEVV AAAREAGVNL
RPTDADHVGI ACDETTGRAQ LAAVWSAFGV DGGNGEGSGI PGIDELDASA PDALPEGLLR
HDGYLAHPVF HQHRSETAML RYLRRLADRD YALDRGMIPL GSCTMKLNAT AEMEPVTWPE
FGALHPFAPA EQAQGYLTLI RELEERLAEV TGYDKVSLQP NAGSQGELAG LLAVRAYHRA
NGDTQRTVCL IPSSAHGTNA ASAVMAGMKV VVVKTGQDGE VDTDDLRAKI EQYGDQLAVL
MVTYPSTHGV FEEHITEICA TVHDAGGQVY VDGANLNALV GLAEPGRFGG DVSHLNLHKT
FCIPHGGGGP GVGPIAVREH LAPYLPNHPL QPAAGPATGV GPVSAAPWGS AGILPISWAY
IRLMGAEGLR RATQVAVLGA NYVAKRLEPH YPVLYTGPGG LVAHECIVDL RPLTKATGVT
VDDVAKRLID YGFHAPTMSF PVAGTLMIEP TESEDLAELD RFCQAMIAIR AEIEKVGSGE
WAKEDNPLRN APHTAASLTA EWDHPYSREE AVFPAGVSAA DKYWPPVRRI DGAYGDRNLV
CSCPPLESYE G
//
