ID A0A0A2LW53_9FLAO Unreviewed; 949 AA.
AC A0A0A2LW53;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=Q763_00135 {ECO:0000313|EMBL:KGO84189.1};
OS Flavobacterium beibuense F44-8.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1406840 {ECO:0000313|EMBL:KGO84189.1, ECO:0000313|Proteomes:UP000030129};
RN [1] {ECO:0000313|EMBL:KGO84189.1, ECO:0000313|Proteomes:UP000030129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F44-8 {ECO:0000313|EMBL:KGO84189.1,
RC ECO:0000313|Proteomes:UP000030129};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) 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:KGO84189.1}.
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DR EMBL; JRLV01000001; KGO84189.1; -; Genomic_DNA.
DR RefSeq; WP_035129661.1; NZ_JRLV01000001.1.
DR AlphaFoldDB; A0A0A2LW53; -.
DR STRING; 1406840.Q763_00135; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR Proteomes; UP000030129; 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:UP000030129}.
FT DOMAIN 9..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 469..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; 104142 MW; 003245508EA67819 CRC64;
MRTDAFALRH IGPRENDLQH MFKTIGVESI DQLIYETLPD DIRLKAPLNL DPAMTEYEYL
NHIHQLGAKN KIFRSYIGLG YHPAIVPAAV QRNIFENPGW YTAYTPYQAE IAQGRLEALL
NFQTTVIELT GMEIANASLL DEGTAAAEAM ALLFDVRTRD QKKNNVNKFF VSEEILPQTL
SVLQTRSTPI GVELVIGNHE EFDFSEEFFG AILQYPGKYG QVYDYAGFIA KAKEKEIKTA
VAADILSLVK LTSPGELGAD VVVGTTQRFG IPMGYGGPHA AYFATKEEYK RSMPGRIIGV
TIDANGNRAL RMALQTREQH IKREKATSNI CTAQVLLAVM AGMYAVYHGP KGLQYIANKV
HASAVTTADA LNKLGVYQTN TSFFDTIVVK ADAAKVKAAA ENKEINFYYI DGETVAIAFN
ETTSLKDIND IVAVFAEATG KTAEAVTALA ETVHIPSTLI RTSEFLSHEV FNKYHSETAL
MRYIKKLERK DLSLNHSMIS LGSCTMKLNA AAEMIPLSYP RWNNIHPFAP LEQAQGYQTM
LKKLEEQLNV ITGFAGTTLQ PNSGAQGEYA GLMVIRAYHQ SRGEDHRNIA LIPASAHGTN
PATANMAGMK VVVTKTSENG NIDVEDLKAK AELHKDNLAC LMVTYPSTHG VYEASIKEIT
QIIHDNGGQV YMDGANMNAQ VGLTNPATIG ADVCHLNLHK TFAIPHGGGG PGVGPICVAA
HLVPFLPTNP VIATGGNNAI TAISAAPWGS ALVCLISYGY ITMLGAEGLT SSTHHAILNA
NYIKERLKGH FQTLYTGEMG RAAHEMIIEC RPFKQNGIEV TDIAKRLMDY GFHAPTVSFP
VAGTLMVEPT ESENLEELDR FCDAMIAIRK EIDEASADDK NNVLKNSPHT LAMLTSDSWD
FPYTREKAAY PLEYLAENKF WPSVRRVDDA YGDRNLVCSC APIEAYMEE
//
