ID A0A2Z5R4U9_9MICC Unreviewed; 948 AA.
AC A0A2Z5R4U9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=RA11412_2590 {ECO:0000313|EMBL:BAV88889.1};
OS Rothia aeria.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=172042 {ECO:0000313|EMBL:BAV88889.1, ECO:0000313|Proteomes:UP000250241};
RN [1] {ECO:0000313|EMBL:BAV88889.1, ECO:0000313|Proteomes:UP000250241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 11412 {ECO:0000313|EMBL:BAV88889.1,
RC ECO:0000313|Proteomes:UP000250241};
RA Nambu T.;
RT "Genome sequence of Rothia aeria strain JCM11412.";
RL Submitted (OCT-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; AP017895; BAV88889.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5R4U9; -.
DR KEGG; raj:RA11412_2590; -.
DR Proteomes; UP000250241; Chromosome.
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:UP000250241}.
FT DOMAIN 5..428
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 445..725
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 766..886
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 689
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 948 AA; 102093 MW; 24B9C89464A251E2 CRC64;
MSFIDRHLGP RSADAEQMLS TLGYDSLGAL MDAVVPEQIR LRADLPLPEP LTEQDALAKI
AGYAAKNKVY AQMIGAGYYD AVTPAVLRRN ILENPGFYTS YTPYQAEISQ GRLEALLNFQ
NTVMELTGLE IANASLLDEA TAVAEAVVMM HRANRKVKNG FFAIDSRCLP QVISVVRGRA
QMLDIPFVIT DFSDGLPEGD LYGVVFAYPA QDGQLRDIEP LIKAAKERKA LVTVVADLLA
LTLLKSPGEL GADVAVGNTQ RFGLPFFFGG PHAAYMAVHK GMERTLPGRL VGVSQDSSGK
PAYRLALQTR EQHIRREKAT SNICTAQALL AIVAGAYAMY HGPEGLRAIA ERLHTNAARV
ATALQKAGYG IVHKNFFDTV VVEAPGAADE LVAKALDAGV NIRRFDANRV GISVGESHGD
AVLGRLVKAL GGELPAEADP AFGIPDALLR TDDYMQHPIF HKYRSETEMM RYLRRLSDKD
LALDRTMIPL GSCTMKLNAA AEMEPISWPE FAGVHPLAPA DQAQGWHELI RELSDWLVAI
TGYDAVSLQP NSGASGEYAG LRAIRSYHEA NGDHQRNTVL IPLSAHGTNA ASAALAGLKV
AGVATASDGS IDVEDLKAKI EKYGDAIAGI MITYPSTHGV FEEQVAQVCE LVHAAGGQVY
VDGANLNAQM GFAQPGKFGG DVSHLNLHKT FSIPHGGGGP GVGPLAVREH LVKYLPGDAY
TADAEGNLPE GAALPIAQAF FGSAGVLPIS WMYIAMSGAE GLKSSSAYAV LNANYVAKKL
NDKFPVLYTG PGGLVGHECI LDVRELTDRS HVTAEDVCKR LMDFGFHAPT LAFPVPGTLM
MEPTESESKE ELDRFIEAME TIYDEILEVA DGKVALEDSV LRNAPHTVEV VSADEWDRPY
TRTQAAYPVK SLRLNKYFTP VGRIDGAGGD RHFVCECPPM EAFDLEAQ
//
