ID A0A1I3M639_9PSEU Unreviewed; 954 AA.
AC A0A1I3M639;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05421835_102186 {ECO:0000313|EMBL:SFI92195.1};
OS Amycolatopsis sacchari.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=115433 {ECO:0000313|EMBL:SFI92195.1, ECO:0000313|Proteomes:UP000199025};
RN [1] {ECO:0000313|EMBL:SFI92195.1, ECO:0000313|Proteomes:UP000199025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44468 {ECO:0000313|EMBL:SFI92195.1,
RC ECO:0000313|Proteomes:UP000199025};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FORP01000002; SFI92195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3M639; -.
DR STRING; 115433.SAMN05421835_102186; -.
DR Proteomes; UP000199025; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199025}.
FT DOMAIN 21..446
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 475..733
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 775..896
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 705
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 954 AA; 102011 MW; 416253A13D700E6E CRC64;
MTEGEFPQPL NEELPMSTFA DRHIGPAEHE QAKMLAECGY GSLDALVDAA VPAGIRTDRD
LRLPPPASEQ EATAELRALA TKNRPMTQMI GLGFSDTVTP PVIRRNVLEN PAWYTAYTPY
QPEISQGRLE ALLNFQTMVS TLTGLDTANA SLLDESTAVA EAVMLMRRQS KAKSSRVVLD
AECLPQTIAV VRTRAEAVGI EVDVRDLHTG LPEDFFGVVV QYPGASGVLR GKGFYEAIGK
VAKEAGALYT VAADLLALTL VTAPGEFGAD VAAGTTQRFG VPLGYGGPHA GYLAVRKGLE
RSLPGRLVGV SVDADGNPAY RLALQTREQH IRREKATSNI CTAQVLPAVL AAMYAVYHGP
DGLKAIAQRV HGLATGLAAA LREGGVEVVH EGFFDTVLAR VPGRAGQVLA DARRFGINLG
RVDDDHVRIA CDEVTTVDTL RRVLLAFDLE AHAEPGPSAL PAGLARESEY LTHEVFHKHR
SETSMLRYLR RLSDQDYALD RGMIPLGSCT MKLNATAEME PISWPEFAGI HPFAPAEDAE
GYRELIDQLC GWLAEVTGYD EVSLQPNAGS QGEFAGLLAI RAYHKANGQP ERDVCLIPSS
AHGTNAASAV LAGMRVVVVA CRENGDVDLE DLKAKVDAHR DTLAAIMVTY PSTHGVYEDG
IGELARIVHE AGGQVYVDGA NLNALLGLAK PGEFGGDVSH LNLHKTFCIP HGGGGPGVGP
VAVRAHLAPY LPGHPNLAGD SAVGPVSAAP YGSASILPIS WAYVRMMGAA GLTAATKVAV
LAANYIAARL APHYPVLYTG RGGLVAHECI LDLRALTKRT GVTVEDVAKR LVDYGFHAPT
MSFPVAGTLM VEPTESEDVA EIDRFCDAMI AIRREIEEVA EGRWPVEQSP LRNAPHTAET
LTSDWDLPYD RKTAVYPAGV SPKGKYWPPV RRIDGAYGDR NLVCSCPPIE AYGS
//
