ID A0A1Q9UY64_9PSEU Unreviewed; 954 AA.
AC A0A1Q9UY64;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BJF85_22260 {ECO:0000313|EMBL:OLT42665.1};
OS Saccharomonospora sp. CUA-673.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=1904969 {ECO:0000313|EMBL:OLT42665.1, ECO:0000313|Proteomes:UP000186761};
RN [1] {ECO:0000313|EMBL:OLT42665.1, ECO:0000313|Proteomes:UP000186761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CUA-673 {ECO:0000313|EMBL:OLT42665.1,
RC ECO:0000313|Proteomes:UP000186761};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
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:OLT42665.1}.
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DR EMBL; MKKE01000035; OLT42665.1; -; Genomic_DNA.
DR RefSeq; WP_075848885.1; NZ_MKKE01000035.1.
DR AlphaFoldDB; A0A1Q9UY64; -.
DR STRING; 1904969.BJF85_22260; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000186761; 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:UP000186761}.
FT DOMAIN 19..444
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 477..729
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 REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 954 AA; 101164 MW; 9094086439A85E18 CRC64;
MTVPAHTPTS SPSSSFMPRH IGPAEPEQAK MLAECGYGSL DALAAAAVPS AIRTTGELDL
PEPASEQEAI SELRALAAKN RPMTQMIGLG YHDTVTPAVI RRNVLEKPAW YTAYTPYQPE
ISQGRLEALL NFQTMVSDLT GLATANASML DEPTAVAEAM MLMRRASKAK SSTIVVDADC
LPQTISVLRT RAEVVGIEVD VRDLTQGLPE EFFGVVVQYP GASGVLRAPE FYAGIGEAAT
AAKALYCVAG DLLALTKVQA PGEFGADLAA GSSQRFGVPM GYGGPHAGYL AVREGLERSL
PGRLVGVSID SAGAPAYRLA LQTREQHIRR EKATSNICTA QVLLAVMASM YAVYHGPDGL
RRIADRVHGH ATTIADALRA GGVEVVHEHF FDTVLARVPG RAGTVVEAAR EAGINLGADG
ADHVRIACDE ATSPQVVDAV LSAFGVANPG AEATIAIPAG LERATDYLTH EVFHSHRSET
AMLRYLRGLS DLDYALDRGM IPLGSCTMKL NATTEMEAVT WPEFANIHPF APAEDAAGYR
ELTDQLSTWL AEVTGYHSVS LQPNAGSQGE LAGLLAIRAY HRANGQPERD VCVIPSSAHG
TNAASAVLAG MRVVVVACTD DGDVDLADLR AKVDQHRDTL AAIMVTYPST HGVYETGISE
LAEIVHEAGG QVYVDGANLN ALLGLAKPGE FGGDVSHLNL HKTFCIPHGG GGPGVGPVAV
REHLAPYLPN HPQFPGAGPE TGVGPISGAP YGSASILPIS WAYVRMMGST GLTSATQVAV
LAANYVAARL SPHYPVLYTG QNGLVAHECI IDLRQLTKQT GVTVDDVAKR LIDYGFHAPT
MSFPVAGTFM VEPTESEDLS ELDRFCDAMI SIRREIAEVA AGTWEVERSP LRGAPHTAEQ
LAGEWDLPYD RALAVYPGNT RAKGKYFSPV RRIEGAYGDR NLVCSCPPVT DFES
//
