ID A0A1A8ZN48_9ACTN Unreviewed; 940 AA.
AC A0A1A8ZN48;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=GA0070621_2301 {ECO:0000313|EMBL:SBT45293.1};
OS Micromonospora narathiwatensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=299146 {ECO:0000313|EMBL:SBT45293.1, ECO:0000313|Proteomes:UP000198765};
RN [1] {ECO:0000313|EMBL:SBT45293.1, ECO:0000313|Proteomes:UP000198765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45248 {ECO:0000313|EMBL:SBT45293.1,
RC ECO:0000313|Proteomes:UP000198765};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; LT594324; SBT45293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A8ZN48; -.
DR PATRIC; fig|299146.4.peg.2376; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000198765; Chromosome i.
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:UP000198765}.
FT DOMAIN 8..432
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 433..722
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 760..881
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 690
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 940 AA; 99752 MW; 3594F3E1A1F028BA CRC64;
MTAEQFADRH IGPDPGDERR MLETVGYSSV DELMDAAIPE VIRWHGTLDL PAPASEREAI
AELRALAARN TVAVSMIGLG YHGTHTPGVI RRNVLENPAW YTAYTPYQPE ISQGRLEALL
NFQTMVTDLT GLATANASML DEGTAAAEAM TLARRASRSK SPVYVVDADA LPQTVAVITS
RAEPLGIDVR VLDLGRDELP AEFFGLHLQY PGASGAVRDH AGLVEAAHRV GALVCVAADL
LALTLLRPPG EIGADIAAGT TQRFGVPMGF GGPHAGYLAV RAGLERMLPG RLVGVSKDAD
GNPAYRLALQ TREQHIRREK ATSNICTAQV LLAVMAGMYA VYHGPDGLRA IARRTHELAA
RLAAGLRAGG VTVADVAFFD TVTATVPGRA AEVVAAAAER NVNLRLVDAD RVGISCDETT
TPAHLAAVWA AFGVPAFDGA GDAALPAGLR RASDFLTHPV FHRHRSETAM LRYLRRLADF
DYALDRGMIP LGSCTMKLNA TTEMEAITWP EFAHLHPFAP AEQTAGYREL IAQLEDWLAE
VTGYDAVSVQ PNAGSQGELA GLLAIRAYHR QRGEGHRDVC LIPSSAHGTN AASAVMAGMR
VVVVGCDADG NVDLVDLDAK IDKHRDDLAA IMVTYPSTHG VYETGIASLC AKVHDAGGQV
YVDGANLNAL VGFAKPGRFG ADVSHLNLHK TFCIPHGGGG PGVGPVAVRA HLAPFLPGDP
AGAVREGRPA ISAARHGSAG ILPIPWAYLR MMGAEGLTRA TGVAVLAANY VAARLRDHFP
VLYAGNKGLV AHECILDLRP LTRASGVSVD DVAKRLIDYG FHAPTMSFPV AGTLMVEPTE
SEDLAELDRF CDAMIAIRAE IDKVASGEWP AGDNPLCNAP HTAAMVSGDE WPHPYPRSVG
AYPAGVDRAG RYWPPVRRID GAYGDRNLVC SCPSPEAFES
//
