ID A0A3A4K1A5_9NOCA Unreviewed; 935 AA.
AC A0A3A4K1A5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:RJO73490.1};
GN ORFNames=D5S18_19960 {ECO:0000313|EMBL:RJO73490.1};
OS Nocardia panacis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=2340916 {ECO:0000313|EMBL:RJO73490.1, ECO:0000313|Proteomes:UP000266677};
RN [1] {ECO:0000313|EMBL:RJO73490.1, ECO:0000313|Proteomes:UP000266677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM PH 21724 {ECO:0000313|EMBL:RJO73490.1,
RC ECO:0000313|Proteomes:UP000266677};
RA Miao C.;
RT "YIM PH21274 draft genome.";
RL Submitted (SEP-2018) 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:RJO73490.1}.
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DR EMBL; QZFU01000023; RJO73490.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A4K1A5; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000266677; 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:UP000266677}.
FT DOMAIN 7..430
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 457..716
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 755..876
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 688
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 935 AA; 99059 MW; 8B727E32A3524DED CRC64;
MTRSFADRHI GPDPDELQRM LSVIGVDSLD DLAAAALPSG ILDGSGLAPL PPAATEHEVL
AELAELAGAN TVATSMLGLG YYDTLTPPVL IRNLLENPAW YTAYTPYQPE ISQGRLEALL
NFQTMVSDLT GMDVANASML DEATAAAEAM TLLRRAGRSS SARLVIDTDL FPQTRTVLYT
RAEPLGIELV EADLAGAGLP EGEFFGVLTQ SPGASGRVVD LTSVIVAAHE RGALVAVGAD
LLAATLITPP GEQGADVCFG TTQRFGVPLG FGGPHAGYLA VRQAHARQLP GRLVGVSVDA
DGATAYRLAL QTREQHIRRE KATSNICTAQ VLLAIVAAMY ASYHGANGLR AIARRVHGHA
AAIAAALGAA VVHERFFDTV LVQAPGVAEA VVAKARSRGI NLRQVDADHV AVACDEATTP
AHVAAVVESF GAAQPVETAA PDRGAIETRT SEFLTHPAFT RYHTETAMLR YLRALSDKDI
ALDRSMIPLG SCTMKLNATA EMEPITWPGF ARVHPYAPVE DAPGLLKVIA DLQNWLCDIT
GYDSVSLQPN AGSQGEYAGL LAIRRYHLDR GDAHRDTCLI PSSAHGTNAA SAAMAGLRVE
VVKCRENGDV DLDDLRAKIA DHADRLACIM ITYPSTHGVY EQEVAELCGL VHEAGGQVYV
DGANLNALVG VARPGKFGGD VSHLNLHKTF CIPHGGGGPG VGPVAVGAHL APYLPGDPLE
SGSHAVSAAK YGSASILPIT WAYIRMMGAD GLRRATLSAI ASANYIARRL DAHFPVLYTG
ENGMVAHECI LDLREITKRT GVTVDDVAKR LADYGFHAPT MSFPVAGTLM VEPTESENLA
EIDEFIAAMI AIRAEIDQVG AGVWPVEDNP LRGAPHTAAC LVGEWTHPYS RETAVYPRGV
AHTRAKVWPS VRRIDGAYGD RNLVCSCPPL EAYQD
//
