ID A0A0L0KD70_9ACTN Unreviewed; 960 AA.
AC A0A0L0KD70;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=IQ63_13885 {ECO:0000313|EMBL:KND35768.1};
OS Streptomyces acidiscabies.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=42234 {ECO:0000313|EMBL:KND35768.1, ECO:0000313|Proteomes:UP000037151};
RN [1] {ECO:0000313|Proteomes:UP000037151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) 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:KND35768.1}.
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DR EMBL; JPPY01000086; KND35768.1; -; Genomic_DNA.
DR RefSeq; WP_050370942.1; NZ_KQ257815.1.
DR AlphaFoldDB; A0A0L0KD70; -.
DR PATRIC; fig|42234.21.peg.2864; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000037151; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037151}.
FT DOMAIN 19..447
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 476..736
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 782..903
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 709
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 960 AA; 102233 MW; CF4528A385689D6B CRC64;
MTPPRTPLSV LEQGVPFEQR HIGPGREAQA KMLAQVGYGS LDELTAAAVP DAIKNVAALD
LPGARSEAQV LAELRELAGR NQVLGSMIGL GYYGTFTPPV ILRNVMENPA WYTAYTPYQP
EISQGRLEAL LNFQTMVADL TGLPTSGASL LDEGTAAAEA MALSLRMGKN KKGLFLVDAD
AFPQTVAVIR TRAEPTGVEV VVADLSDGIP AEVAGREING VLIQYPGASG VVRDIKPLVE
QAHAVGALVT VAADLLALTL LTSPGELGAD IAVGTTQRFG VPMGFGGPHA GYMAVHEKFA
RSLPGRLVGV SVDADGNRAY RLALQTREQH IRREKATSNI CTAQVLLAVM AGMYAVYHGP
DGLRQIAWKT HRYATVLAEG LRIGGVDVVH QAYFDTVLAR VPGGAAQVVD AARDGGVNLR
LVDEDLVSIA CDETTTRAQL GIVWQAFGVS GDVDSFDASA REGLGDDVLR RDEVLSHPVF
HQHRSETAML RYLRRLADRD YALDRGMIPL GSCTMKLNAT TEMEPVTWPE FGQLHPFAPV
EQAGGYLTLI RELEDQLAEV TGYDKVSLQP NAGSQGELAG LLAVRAYHRA NGDLQRTVCL
IPSSAHGTNA ASAVMAGMKV VVVKTSEDGE VDVEDLRGKI GQYRDELAVL MITYPSTHGV
FEEHVGEICG LVHEAGGQVY VDGANLNALV GVAKPGHFGG DVSHLNLHKT FCIPHGGGGP
GVGPVAVRAH LAPYLPNHPL QSEAGPATGV GPVSAAPWGS AGILPISWAY VRLMGGEGLK
RATQVAVLSA NYIAKRLEPH YPVLYTGPGG LVAHECIIDL RPLTKATGVS VDDVAKRLID
YGFHAPTMSF PVAGTLMIEP TESEDLAELD RFCAAMIAIR GEIEKVGAGE WGADDNPLRN
APHTAAALSG EWDHSYTREE AVFPGEGAVS EKYWPPVRRI DQAYGDRNLV CSCPPLESYQ
//
