ID A0A3P3W6X3_9FLAO Unreviewed; 949 AA.
AC A0A3P3W6X3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ECO:0000313|EMBL:RRJ90935.1};
GN ORFNames=EG240_07890 {ECO:0000313|EMBL:RRJ90935.1};
OS Paenimyroides tangerinum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Paenimyroides.
OX NCBI_TaxID=2488728 {ECO:0000313|EMBL:RRJ90935.1, ECO:0000313|Proteomes:UP000275719};
RN [1] {ECO:0000313|EMBL:RRJ90935.1, ECO:0000313|Proteomes:UP000275719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 102701-2 {ECO:0000313|EMBL:RRJ90935.1,
RC ECO:0000313|Proteomes:UP000275719};
RA Li G., Jiang Y.;
RT "Flavobacterium sp. nov., YIM 102701-2 draft genome.";
RL Submitted (NOV-2018) 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:RRJ90935.1}.
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DR EMBL; RQVQ01000014; RRJ90935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P3W6X3; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000275719; Unassembled WGS sequence.
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; 1.
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:UP000275719}.
FT DOMAIN 9..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 469..729
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; 104242 MW; D430DFAF3C7A91E9 CRC64;
MKTNAFALRH IGPRPTDLQH MFNTVGVKDI DQLLFETFPD KIRLQKDLEL DPAMTEYEYM
SHITELGSKN KVYRSMIGLG YHEAIVPAVI QRNIFENPGW YTAYTPYQAE IAQGRLEALL
NFQTTVIELS GMEIANASLL DESTAAAEAM ALLFDVRTRD QKKNNANKFF VSEEVLPQTL
SVLQTRSTPI GIELVVGNHE TFDFSEDFFG VMLQYPGKFG QIHDYGDFIN TAKTKDIKVA
VAADILSLVR LKSPGEMGAD VVVGTTQRFG IPLGFGGPHA GFFATKEEYK RSMPGRIIGV
SQDANGNRAL RMALQTREQH IKREKATSNI CTAQVLLAVM AGMYAVYHGP NGLRFIANNV
HATAVTIETE LAQLGFEQVN DAYFDTILVK ADAAKIKEVA EKNNYNFFYA DANHVSISVN
ETTSLKDINN IVAIFAEVAG KSFETVTELS GLALVPVSLE RTSAFLEHEV FNTHQSESQL
MRYIKKLERK DLALNHSMIS LGSCTMKLNA AAEMLPLSLP NWNNMHPFAP ASQAEGYLTM
LHKLEEQLNV ITGFAGTTLQ PNSGAQGEYA GLMVIRAYHE SRGEGHRNIA LIPSSAHGTN
PASAAMAGMK VVVTKTTEEG NIDVEDLRAK AEQYKDSLSC VMITYPSTHG VYESSIIEIT
SFIHENGGQV YMDGANMNAQ VGLTNPATIG ADVCHLNLHK TFAIPHGGGG PGVGPICVAQ
HLVEFLPTNP IVKVGGDNAI TAISAAPYGS ALVCLISYGY ISMLGAEGLR KSTETAILNA
NYMKARLQEG YEVLYSGERG RAAHEMIIDC RMFKSQGIEV TDIAKRLMDY GFHAPTVSFP
VAGTLMIEPT ESEDLAELDR FCDAMLSIRK EIEAATAEDT NNVLKNAPHT LAMLTAETWE
QPYSRQQAAY PLEYVSENKF WPTVRRIDDA YGDRNLVCSC APIEAYMEA
//
