ID F8JU68_STREN Unreviewed; 961 AA.
AC F8JU68; G8WVZ1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
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 OrderedLocusNames=SCATT_07130 {ECO:0000313|EMBL:AEW93084.1};
OS Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925
OS / NBRC 14057 / NRRL 8057) (Streptomyces cattleya).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptantibioticus.
OX NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW93084.1, ECO:0000313|Proteomes:UP000007842};
RN [1] {ECO:0000313|Proteomes:UP000007842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC {ECO:0000313|Proteomes:UP000007842};
RA Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL Submitted (DEC-2011) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003219; AEW93084.1; -; Genomic_DNA.
DR RefSeq; WP_014141480.1; NC_017586.1.
DR AlphaFoldDB; F8JU68; -.
DR STRING; 1003195.SCATT_07130; -.
DR KEGG; scy:SCATT_07130; -.
DR PATRIC; fig|1003195.11.peg.2312; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_3_2_11; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000007842; Chromosome.
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:UP000007842}.
FT DOMAIN 19..447
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 454..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 961 AA; 101569 MW; 5FC48B37CE5B76E3 CRC64;
MTANRIPLAD LERGTPFEER HIGPDAGAQA KMLAHVGYGS LDELTAAAVP DAIKSAEALA
LPAARTEADV LAELRSLAGR NQVLSSMIGL GYYGTFTPPV ILRNVMENPA WYTAYTPYQP
EISQGRLEAL LNFQTMVADL TGLPTSGASL LDEGTAAAEA MALSRRVGKV KDGVFLVDAD
CFPQTVAVVE TRAEPTGVEV VVADLTDGIP AEVAERGVFG VLLQYPGASG AVRDPRPVIE
RAHELGAVVT VAADLLALTL LTPPGELGAD IAVGTTQRFG VPMGFGGPHA GYMAVRDQFA
RSLPGRLVGV SVDADGDRAY RLALQTREQH IRREKATSNI CTAQVLLAVM AGMYAVHHGP
DGLTGIARKV HRYAAVLAAG LRAGGVEVAH DAFFDTLTAR VPGRAAEVVA AARTAGVNLR
LVDADRVGVS CDETTGRGQL AAVWQAFGVT GDVDALDAET GDALPAELAR TSGFLAHPVF
HQHRSETAML RYLRRLADRD YALDRGMIPL GSCTMKLNAT AEMEPVTWPE FASLHPFAPA
EQAEGYLTLI HELEERLAAI TGYDKVSLQP NAGSQGELAG LLAVRAYHRA NGDTGRTVCL
IPSSAHGTNA ASAVMAGMRV VVVRTGEDGE VDTADLRAKI EQYGDELAVL MVTYPSTHGV
FEEHIGEICA LVHDAGGQVY VDGANLNALV GLARPGRFGG DVSHLNLHKT FCIPHGGGGP
GVGPVAVRAH LAPYLPNHPL QPTAGPGTGV GPVSAAPWGS AGILPISWAY ARLMGADGLK
RATQVAVLSA NYLAKRLAPY FPVLYTGPGG LVAHECIIDL RPLTKATGVT VDDVAKRLID
YGFHAPTMSF PVAGTLMIEP TESEDLAELD RFCEAMIAIR AEIDRVGSGE WPKDDNPLRN
APHTAAMLGG EWEHAYPRQE AVFPAGVSAA DKYWPPVRRI DGAFGDRNLV CSCPPLEEYE
G
//
