ID I1D0A0_9PSEU Unreviewed; 952 AA.
AC I1D0A0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=SacglDRAFT_01451 {ECO:0000313|EMBL:EIE98374.1};
OS Saccharomonospora glauca K62.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=928724 {ECO:0000313|EMBL:EIE98374.1, ECO:0000313|Proteomes:UP000005087};
RN [1] {ECO:0000313|EMBL:EIE98374.1, ECO:0000313|Proteomes:UP000005087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K62 {ECO:0000313|EMBL:EIE98374.1,
RC ECO:0000313|Proteomes:UP000005087};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Brambilla E., Klenk H.-P., Woyke T.J.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K62 {ECO:0000313|Proteomes:UP000005087};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA Klenk H.-P., Woyke T.;
RT "Noncontiguous Finished sequence of chromosome of Saccharomonospora glauca
RT K62.";
RL Submitted (JAN-2012) 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; CM001484; EIE98374.1; -; Genomic_DNA.
DR RefSeq; WP_005463027.1; NZ_CM001484.1.
DR AlphaFoldDB; I1D0A0; -.
DR STRING; 928724.SacglDRAFT_01451; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_2_2_11; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000005087; 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:UP000005087}.
FT DOMAIN 11..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 468..722
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 768..889
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 695
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 952 AA; 101539 MW; 4121FDDDFA430C1B CRC64;
MSHSSTPFAS RHVGPGTSER AKMVAECGFD SLDALVAAAV PSAIRTDGEL RLPAPVSEEQ
ALAELRELAR RNRPMTQMIG LGYYDTVTPA VIRRNVLENP AWYTAYTPYQ PEISQGRLEA
LLNFQTAVSD LTGLAIANAS LLDESTAVAE AMMLMKRASK SKSNTVVVDA ECLPQTVAVV
RTRAQAVGIE VDVRDLSHGL PDEFFGVVVQ YPGASGVLRD PDFYREIGEA AKRVKALYCV
AADLLALTLL TAPGEFGADV AAGTTQRFGV PLGYGGPHAG YLAVRSGLER SLPGRLVGVS
VDAAGAPAYR LALQTREQHI RREKATSNIC TAQVLLAVVA SMYAVYHGPE GLRRIAERVH
GHAVALADAL RAGGVEVVHD HFFDTVLARV PGRAEEVLAA AREAGVNLGG VDADHVRVAC
DEVTTPEVLA TVLGAFGVRA TPEPASRSAF PSGLERTSAY LTHEVFHSYR SETAMLRYLR
RLADYDYALD RGMIPLGSCT MKLNATTEME PITWPEFANI HPFAPAEDAE GYRELIGQLS
RWLAEVTGYD SVSLQPNAGS QGELAGLLAI RAYHRANGQP ERDVCLIPAS AHGTNAASAV
LAGMRVVVVA CTDDGDVDLT DLRAKVDAHR DTLAAIMVTY PSTHGVYETG IGELAEIVHE
AGGQVYVDGA NLNALLGLAK PGEFGGDVSH LNLHKTFCIP HGGGGPGVGP VAVRAHLAPY
LPNHPLAPEA GPETGVGPIS AAPFGSASIL PISWAYVRMM GAAGLTEATK VAVLNANYVA
ARLAPHYPVL YTGRDGLVAH ECILDLRGLT KRTGVTVDDV AKRLIDYGFH APTMSFPVPG
TLMVEPTESE DLAELDRFCE AMISIRREID EVANGTWAVE DSPLRNAPHT AEQLAGEWTL
PYDRRTAVYP GRTSPKGKYW SPVRRIEGAY GDRNLVCSCP PVSSYESAGS VS
//
