ID A0A1H1P0H9_9FLAO Unreviewed; 949 AA.
AC A0A1H1P0H9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN04515667_1288 {ECO:0000313|EMBL:SDS04712.1};
OS Formosa sp. Hel1_31_208.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1798225 {ECO:0000313|EMBL:SDS04712.1, ECO:0000313|Proteomes:UP000199458};
RN [1] {ECO:0000313|EMBL:SDS04712.1, ECO:0000313|Proteomes:UP000199458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_31_208 {ECO:0000313|EMBL:SDS04712.1,
RC ECO:0000313|Proteomes:UP000199458};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; LT629733; SDS04712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1P0H9; -.
DR STRING; 1798225.SAMN04515667_1288; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000199458; Chromosome i.
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 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:UP000199458}.
FT DOMAIN 9..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 465..727
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 772..889
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 700
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 949 AA; 104635 MW; CEBB7A72BAD00590 CRC64;
MNTADFSLRH IGPRAADQKQ MLDTIGVDSM EQLIHETIPN GIRLDSDLDL EAPMSEHEYL
LHIYELSKKN KVFKTYIGLG YHPTILPAVI QRNILENPGW YTAYTPYQAE IAQGRLEALL
NFQTMITDLT GMEIANASLL DESTAAAEAM SLLFAVRERD QKKAGINKFF VSENILPQTL
SLLQTRATPI GIELVIGKEE DFDFSESYFA AILQYPGKYG QVTDIKSFIE KANASNIKVA
VAADIMSLVK LEAPGKFGAD VVVGTTQRFG IPMGYGGPHA AYFATKKAYK RDLPGRIIGV
TKDTNGHRAL RMALQTREQH IKRDKATSNI CTAQVLLAVM AGMYAVYHGP KGLEQIANDI
HNKTVSLSNT LKTLGFQQSN TSFFDTLHIQ ADAKAIKIDA ESHKINFFYP NENEVVLSLN
ETTTVDDLNA IVSIFAKSIN TNTSEIETIS EANVITPNLK RQSTFLQEPI FNSHHSETEL
MRYIKLLERK DLALNHSMIS LGSCTMKLNA ASEMLPLSWF KWGNIHPFVP IAQAQGYQIV
LKELEDQLTE ITGFAGTSLQ PNSGAQGEFA GLMVIRAYHE SRGDHHRNIC IIPSSAHGTN
PASAVMAGMK VVVTKSTEEG NIDVDDLREK AELHAANLSA LMVTYPSTHG VYESAIKEIT
QIIHDNGGQV YMDGANMNAQ VGLTHPGNIG ADVCHLNLHK TFAIPHGGGG PGVGPICVAK
QLVPFLPSNP LIKTGGDQAI TAISAAPFGS SLACLISYGY IKMLGATGLK RATEVAILNA
NYIKKRLEGA FETLYSGERG RAAHEMIIDC RPFKAHGIEV VDIAKRLMDY GFHAPTVSFP
VAGTMMIEPT ESESKDEMDR FCDAMISIRH EIERISKEDD NNILKNAPHT LSMITDDEWL
LPYTRQQAAF PLDYVRDNKF WPSVRRVDDA YGDRNLICTC APIEMYMEA
//
