ID A0A1Q8CL47_9PSEU Unreviewed; 966 AA.
AC A0A1Q8CL47;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=BU204_23755 {ECO:0000313|EMBL:OLF15085.1};
OS Actinophytocola xanthii.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae.
OX NCBI_TaxID=1912961 {ECO:0000313|EMBL:OLF15085.1, ECO:0000313|Proteomes:UP000185596};
RN [1] {ECO:0000313|EMBL:OLF15085.1, ECO:0000313|Proteomes:UP000185596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11-183 {ECO:0000313|EMBL:OLF15085.1,
RC ECO:0000313|Proteomes:UP000185596};
RA Wang W., Yuan L.;
RT "The draft genome sequence of Actinophytocola sp. 11-183.";
RL Submitted (DEC-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}.
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:OLF15085.1}.
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DR EMBL; MSIE01000045; OLF15085.1; -; Genomic_DNA.
DR RefSeq; WP_075127945.1; NZ_MSIE01000045.1.
DR AlphaFoldDB; A0A1Q8CL47; -.
DR STRING; 1912961.BU204_23755; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000185596; 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:UP000185596}.
FT DOMAIN 19..452
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 460..742
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 788..909
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 47..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 715
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 966 AA; 102905 MW; 1556D80B15FD4A4E CRC64;
MTQARIPLAA LEDGTQFADR HIGPRADEVA RMLDVIGVGS LEELADQAVP ASIRDSGQDD
GADDSGETEL PPAVPEHVSL AELRELAGRN ELHTQMIGLG YYGTLTPAVI RRNVLESPAW
YTAYTPYQPE ISQGRLEALL NFQTMVADLT GMELANASML DESTAAAEAM TLLRRAGRAP
SARFLVDADT FPQTIAVIET RAEPLGIEVE VVDLTAGLPE GDFFGLLLSQ PAASGAVRDD
SALVEAAHER GAQVVVAADI LSLTLLRPPG EIGADVVVGS TQRFGVPMGF GGPHAGYLAV
RKGLERQLPG RLVGVSVDAD GNRAYRLALQ TREQHIRREK ATSNICTAQV LLAIVASMYA
VYHGPEGLRS IATRTHRMAA VLAAGLRAGG VEVVHDTFFD TLTLRLPGRA AEVVASARDR
GINIRHVSAD LVSVACDETT TRTHLKKLWA AFGVSGADVD ALDAETADAY PAELARTSAY
LTHPVFSTHR SETSLLRYLR ALSDKDVALD RSMIPLGSCT MKLNATAEME PITWPAFAEL
HPFAPASDAA GLLRVVADLE GWLARLTGYD AVSLQPNAGS QGEFAGLLAI RAYHRSRGES
ARDVCLIPAS AHGTNAASAA MAGMRVVVVR CDDEGNIDLD HLRSTVDQHR ADLACIMITY
PSTHGVYEDT VREVCAAVHD AGGQVYVDGA NLNALIGLAR FGRFGADVSH LNLHKTFCIP
HGGGGPGVGP IGVREHLAPF LPNHPLQPAA GPATGVGPIS AAPWGSASIL PISWAYVRMM
GFEGLRRATM TAVAAANYVA ARLTGHYPVL YTGAHGRVAH ECILDLRGIT KASGITVDDV
AKRLADYGLH APTMSFPVAG TLMVEPTESE DLAELDRFCD AMIAIRREIE RVAAGDWPAE
DNPLRNAPHT AESIAGKWDH PYSREEAAYP TGSTGPKLWP PVRRIDGAKG DRNLVCSCPP
IEAYQS
//
