ID A0A2G1VSJ5_9FLAO Unreviewed; 947 AA.
AC A0A2G1VSJ5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:PHQ29439.1};
GN ORFNames=CJ305_08960 {ECO:0000313|EMBL:PHQ29439.1};
OS Leeuwenhoekiella nanhaiensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Leeuwenhoekiella.
OX NCBI_TaxID=1655491 {ECO:0000313|EMBL:PHQ29439.1, ECO:0000313|Proteomes:UP000229433};
RN [1] {ECO:0000313|EMBL:PHQ29439.1, ECO:0000313|Proteomes:UP000229433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G18 {ECO:0000313|EMBL:PHQ29439.1,
RC ECO:0000313|Proteomes:UP000229433};
RA Liu Q.;
RT "The whole genome shortgun sequences of strain Leeuwenhoekiella nanhaiensis
RT G18 from the South China Sea.";
RL Submitted (AUG-2017) 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:PHQ29439.1}.
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DR EMBL; NQXA01000004; PHQ29439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G1VSJ5; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000229433; 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; 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 9..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 449..730
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 947 AA; 103922 MW; A955A2AE4522C3A6 CRC64;
MRTDVFALRH IGPRPEEKEQ MLEAIGAASI DQLIYETLPD GIKLQKPLNL EPALSEYEYA
THINALANKN KLFKTYIGLG YHESKTPAVI QRNILENPGW YTAYTPYQAE IAQGRLEALL
NFQTMVADLT GMELANASLL DEATAAAEAM TLLAGVRTRD QKKNRTSKFF VDKDIFPQTL
SVLQTRAIPV GVELVVGRAQ EFDFSDEFFG ALIQYPSATG EIHDYTGFIK KAHDLDIKVA
VAADLMSLVL LEAPGKLGAD VVVGTTQRFG IPLGYGGPHA AYFATREEYK RNIPGRIIGV
SKDMNGDRAL RMALQTREQH IKRDKATSNI CTAQVLLAVM AGMYGVYHGP KGLQYIATKI
HRTAATLTDA LENLGLYQLN SGYFDTIRVK ADAKTVRTYA EANEINFYYP DEDTVSIAVN
EATSLADLNK IISVFAEALG KEFTHLEALK ELNAVPDLLQ RESEFMTNEV FNSYHSETEL
MRYIKKLERK DLSLNHSMIS LGSCTMKLNA AAEMLPLSDA RWGGIHPFVP VNQAEGYQYV
LKKLEEQLTE ITGFAATSLQ PNSGAQGEYA GLMVIRAYHE SRGEAHRNIC LIPSSAHGTN
PASAVMAGMQ VVVTKATDAG NIDVDDLREK AEQYKDNLAA LMVTYPSTHG VYESAIQEIT
GIIHEHGGQV YMDGANMNAQ VGLTNPGKIG ADVCHLNLHK TFAIPHGGGG PGVGPICVAE
QLVPFLPGNP VIKTGGAEAI TAISAAPWGS SLVCLISYAY IKMLGATGLK ESTEAAILNA
NYIKERLKGK FEVLYSGEMG RAAHEMIIDC RPFKENGIEV VDIAKRLIDY GFHAPTVSFP
VAGTMMIEPT ESESKAELDR FCDAMINIRK EIDAASADEP NNVLKNAPHT LSMLTADTWD
LPYTREQAAY PLEYVADNKF WPSVRRVDDA FGDRNLICTC APIEEYM
//
