ID A0A285QE65_9ACTN Unreviewed; 966 AA.
AC A0A285QE65;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN06272789_0775 {ECO:0000313|EMBL:SOB80111.1};
OS Streptomyces sp. 1331.2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938835 {ECO:0000313|EMBL:SOB80111.1, ECO:0000313|Proteomes:UP000219030};
RN [1] {ECO:0000313|Proteomes:UP000219030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1331.2 {ECO:0000313|Proteomes:UP000219030};
RA Varghese N., Submissions S.;
RL Submitted (JUL-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}.
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DR EMBL; OBMJ01000001; SOB80111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285QE65; -.
DR Proteomes; UP000219030; Unassembled WGS sequence.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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:UP000219030}.
FT DOMAIN 27..455
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 470..741
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 787..908
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 714
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 966 AA; 102512 MW; E8B80AFA596E4E36 CRC64;
MNAQPNAGRP TGASTLTELE LASPFENRHI GPDAAAQEKM LASVGYASLD ELAATAVPEA
IRSITGLDLP AGRTEAQVLA ELRELAGRNQ VLQPMIGLGY YGTFTPPVIL RNVMENPAWY
TAYTPYQPEI SQGRLEALLN FQTLVSDLTG LPTSGSSLLD EGTAAAEAMA LARRVTKVKG
GVFLVDAETL PQTIAVINTR AVPTGVEVVV ADLSEGIPAE IAERGVFGVL LQYPGATGVV
RDLAPVIEQA HGLGAIVAVA ADLLALTLLK SPGSLGADIA CGTSQRFGVP MGFGGPHAGY
LSVRAEYARS LPGRLVGVSV DSDGNRAYRL ALQTREQHIR REKATSNICT AQVLLAVMAS
MYAVYHGPDG LADIARRTHR YAAALAEGLR AGGVELLHGE FFDTVTAVVP GRAAEIAAAA
RANGINLYQD GEDRISVSTD ETTTREHLAG VWAAFGVPAV EVAEAAETLP AALLREDEYL
THPVFHSHRS ETAMLRYLRR LSDRDYALDR GMIPLGSCTM KLNATTEMEA VTWPEFGQLH
PFAPIEQAQG YLTLIRQLEQ QLVEVTGYDA VSIQPNAGSQ GELAGLLAVR AYHHANGDTQ
RDVCLIPSSA HGTNAASAVM AGMRVVVVKT LVDGDVDVED LKAKIEQHRD TLSVLMVTYP
STHGVYETEI TTICAMVHEA GGQVYVDGAN LNALVGLAKP GKFGADVSHL NLHKTFCIPH
GGGGPGVGPV AVRAHLAPYL PNHPLQSEAG PATGVGPISA APWGSAAILP ISWAYVRLMG
GEGLKRATQV AVLNANYIAK RLAPHFPVLY TGPGGLVAHE SIIDLRPLTK ETGVTVDDIA
KRLIDYGFHA PTMSFPVAGT LMIEPTESED LHEIDRFCDA MIAIRAEIDK VGSGEWAADD
NPLRNAPHTA AELAGDWAHG YSRQEAVFPA GVNPADKYWP PVSRIDGAYG DRNLVCSCPP
LDEYGV
//
