ID A0A0K2YKR3_9NOCA Unreviewed; 951 AA.
AC A0A0K2YKR3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 ECO:0000313|EMBL:CRK51305.1};
GN ORFNames=RHCRD62_20744 {ECO:0000313|EMBL:CRK51305.1};
OS Rhodococcus sp. RD6.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=260936 {ECO:0000313|EMBL:CRK51305.1, ECO:0000313|Proteomes:UP000044872};
RN [1] {ECO:0000313|EMBL:CRK51305.1, ECO:0000313|Proteomes:UP000044872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RD6.2 {ECO:0000313|EMBL:CRK51305.1,
RC ECO:0000313|Proteomes:UP000044872};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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; CVQP01000005; CRK51305.1; -; Genomic_DNA.
DR RefSeq; WP_050064474.1; NZ_CVQP01000005.1.
DR AlphaFoldDB; A0A0K2YKR3; -.
DR STRING; 260936.RHCRD62_20744; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000044872; 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; 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:UP000044872}.
FT DOMAIN 15..445
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 621..732
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 774..895
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 704
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 951 AA; 100981 MW; 47D251D93A37D075 CRC64;
MPDQPTFDPA DFALRHIGPD HTELERILHV IGVDTLDTLA EKAIPGSILD AVTDGVSAGL
DTLPAAVSEH EVLAELAALA ARNTVATSMI GLGYYDTLTP PVLVRNLIEN PAWYTAYTPY
QPEISQGRLE ALINFQTMVS DLTGMEVANS SMLDEATAAA EAMTLLRRAG RSKSPRFVVD
ADLFPQTRAV IETRATPLGI EVVEADLSLG LPEGDFFGVL AQVPGASGRV VDHSSLISAA
HERGALVAVG ADLLALTLLT PPGEMGADAC FGTTQRFGVP MGFGGPHAGY LAVHSKHARQ
LPGRLVGVSV DADGDKAYRL ALQTREQHIR REKATSNICT AQVLLAVVAA MYASYHGAEG
LTAIARRVNG YARTLAAGLR AGGIDVVHTD FFDTVLARVP GRADDVVSAA KGWNVNLRLV
DADHVGIACD EATTTAHLQS VLAAFGVAGD LAGDAAESMP PALARTSEFL THPAFRSHRT
ETAMMRYLRK LSDKDIALDR SMIPLGSCTM KLNAAAEMEA ITWPQFNSLH PFAPADDTVG
IRGLVADLES WLASVTGYDR VSLQPNAGSQ GEYAGLLAIR NYHLSRGDDH RDTCLIPSSA
HGTNAASAVM AGMRVEVVAC RPNGDVDLDD LRAKIADHAE RLAAIMITYP STHGVYEHEV
TEICAAVHDA GGQVYVDGAN LNALVGLARP GRFGGDVSHL NLHKTFCIPH GGGGPGVGPV
AVREHLAPFL PGHPLAPELG DGPTVSAAPY GSASILPITW AYIRMMGAAG LRSASLTAIA
SANYIARRLD EHFPVLYTGD NGMVAHECII DLRQITKDTG VTVDDVAKRL ADYGFHAPTM
SFPVAGTLMI EPTESENLAE IDRFCDAMVS IRREIDRVGA GEWPVDDNPL RGAPHTAACL
VGEWDHPYSR ELAVFPAGTA DKIWPPVRRI DGAHGDRNLV CSCPPIEAFS S
//
