ID A0A2M9BWE5_9MICO Unreviewed; 975 AA.
AC A0A2M9BWE5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CLV54_2041 {ECO:0000313|EMBL:PJJ62244.1};
OS Compostimonas suwonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Compostimonas.
OX NCBI_TaxID=1048394 {ECO:0000313|EMBL:PJJ62244.1, ECO:0000313|Proteomes:UP000230161};
RN [1] {ECO:0000313|EMBL:PJJ62244.1, ECO:0000313|Proteomes:UP000230161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25625 {ECO:0000313|EMBL:PJJ62244.1,
RC ECO:0000313|Proteomes:UP000230161};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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:PJJ62244.1}.
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DR EMBL; PGFB01000003; PJJ62244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9BWE5; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000230161; 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:UP000230161}.
FT DOMAIN 8..443
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 470..731
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 796..917
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 702
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 975 AA; 103819 MW; 672FE28AA06E362E CRC64;
MSDAFVTRHI GTDEAAQQTM LARLGYESVD ALVDAAVPAS IHVDGFRAAT QSVLPPAATE
RETLAELRSF AARNRVNRSM IGLGYYDTIT PSVIKRNVFE NPSWYTAYTP YQPEISQGRL
EALINFQTMI AELTGLDTAN ASMLDEGTAV VEGMMLARRA SRSQSNRFVV DHDALPQTKA
LLTARAAAVG IEIVEVQLDR LDHPTAHGHP LEDAFGVFVQ YPGASGRVWN PKDIIEVAHH
CGALAVVAAD LLALTLLASP GELGADIAVG TSQRFGVPMG FGGPHAGYMA VRAGLERQLP
GRLVGVSVDA AGHPAYRLSL QAREQHIRRE KATSNICTAQ VLLAIMAGMY AVYHGPDGLR
HIAEQVHGTT AALADALEDG GLDLEHEDYF DTIRVRVPGR AAQIVDAAHA AGVNLHLSSE
DCVGISVDET TSDDDIATVL AAFGVEEAWD YAIARNFPVE LARQSAYLTH PVFTTHRSET
SMMRYLKYLA DKDYALDRGM IPLGSCTMKL NAATEMEAVS WPEFAGIHPF APAQDVAGYL
DLIGQLETWL ADVTGYDSVS LQPNAGSQGE LAGLLAIRGY HLSRGDAGRT VCLIPSSAHG
TNAASAVLAG MRVVVVACDE LGNVDLDDLR AKIAEHADAL AALMITYPST HGVYEREVGA
ICRAVHEAGG QVYVDGANLN ALLGFARFGD FGGDVSHLNL HKTFCIPHGG GGPGVGPVAA
KSHLAPFLPG HPLAQSAEHY LRADAGDAGS DAATPDAATV VHAGGPVSAA PYGSPSILPI
SWAYVRMMGA GGLKRATGAA VLAANYVASR LGEHFPVLYT GDSGLVAHEC ILDLRPLTQA
TGVTVDDVAK RLIDYGFHAP TMSFPVAGTL MVEPTESEDL AEIERFIEAM IEIKAEADAV
GAGVWPVDDS PLRGAPHTAE SIVMGEWAHP YDRERAVYPV RSLVRNKYWP PVRRIDQAYG
DRNLVCACPP PEAFE
//
