ID A0A418SKT7_9RHOB Unreviewed; 950 AA.
AC A0A418SKT7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:QPM90967.1};
GN ORFNames=PSAL_022100 {ECO:0000313|EMBL:QPM90967.1};
OS Pseudooceanicola algae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1537215 {ECO:0000313|EMBL:QPM90967.1, ECO:0000313|Proteomes:UP000283786};
RN [1] {ECO:0000313|EMBL:QPM90967.1, ECO:0000313|Proteomes:UP000283786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lw-13e {ECO:0000313|EMBL:QPM90967.1,
RC ECO:0000313|Proteomes:UP000283786};
RA Poehlein A., Wolter L., Daniel R., Brinkhoff T.;
RT "Genome sequence of Rhodobacteraceae bacterium Lw-13e.";
RL Submitted (AUG-2020) 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; CP060436; QPM90967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418SKT7; -.
DR KEGG; palw:PSAL_022100; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000283786; Chromosome.
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:UP000283786}.
FT DOMAIN 16..439
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 468..731
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 768..888
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 701
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 950 AA; 102580 MW; A7F3605554E94A1E CRC64;
MVFTPTDYRP YDFANRRHIG PSPSEMEEML GVIGVEDLET LIGQTVPRQI RQDAALDFGP
ALSEADLLKF MRGVAGKNTV LTSLIGQGYH DTITPPAIKR NILENPAWYT AYTPYQPEIS
QGRLEALLNY QTMICDLTGL DIANASLLDE STAAAEAMTM AQRVAKSKAK AFFVDENCHP
QNIDVIRTRA EPLGIEIILG APGDLQADTV FGAVFQYPGT HGGLTDFTAQ MEALHAAKAL
GVVIADPMAL CILKEPGAMG ADIAVGSTQR FGVPLGYGGP HAAYMACRDA YKRSMPGRIV
GVSIDARGNR AYRLALQTRE QHIRREKATS NVCTAQALLA VMASMYAVFH GPDGLKGISQ
RIHRKTVRLA KGLQDAGFEV GPKAYFDTIH VEVGALQSAV MKSALDEGLN LRRVGTTKVG
ITLDECTRPQ TIEAVWRAFG LSLPGAASEG PYDYLIPDDL ARQTSYLTHE IFHMNRAETE
MMRYMRRLAD RDLALDRAMI PLGSCTMKLN AAVEMEPISW PEFSALHPFC PADQAAGYGQ
LLTDLSAKLC DITGYDAFSM QPNSGAQGEF AGLLTIRNYH KARGEGHRNI CLIPTSAHGT
NPASAQMAGW KVVPVKARDN GDIDLGDFLE KAQKYADDLA ACMITYPSTH GVFEETVREV
CKITHDHGGQ VYIDGANMNA MVGLARPGDI GGDVSHLNLH KTFCIPHGGG GPGMGPIGVG
AHLAEHLPGH VATGGSGAVA AAPYGSPSIL PISWAYCLLM GGEGLTQATR VAILNANYIA
ARLKGAYEVL YKGPQGRVAH ECILDTRPFA DLGVTVDDIA KRLIDCGFHA PTMSFPIAGT
LMVEPTESET RAELDRFCDA MLAIRAEIAS VEDGSTTADA SPLHFAPHTV EDLVAADWNR
DYPREQGCFP PGAFRVDKYW PPVNRVDNVW GDRNLTCTCP PMSDYAEAAE
//
