ID K6WE79_9ACTN Unreviewed; 964 AA.
AC K6WE79;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:GAB90497.1};
GN ORFNames=GORHZ_104_00270 {ECO:0000313|EMBL:GAB90497.1};
OS Gordonia rhizosphera NBRC 16068.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1108045 {ECO:0000313|EMBL:GAB90497.1, ECO:0000313|Proteomes:UP000008363};
RN [1] {ECO:0000313|EMBL:GAB90497.1, ECO:0000313|Proteomes:UP000008363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16068 {ECO:0000313|EMBL:GAB90497.1,
RC ECO:0000313|Proteomes:UP000008363};
RA Takarada H., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA Ohji S., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia rhizosphera NBRC 16068.";
RL Submitted (AUG-2012) 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}.
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:GAB90497.1}.
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DR EMBL; BAHC01000104; GAB90497.1; -; Genomic_DNA.
DR RefSeq; WP_006333312.1; NZ_BAHC01000104.1.
DR AlphaFoldDB; K6WE79; -.
DR STRING; 1108045.GORHZ_104_00270; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000008363; 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:UP000008363}.
FT DOMAIN 14..448
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 473..732
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 774..903
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 964 AA; 102801 MW; A7B00901BA264436 CRC64;
MPPVPESVRS AFVDRHVGPD AGETARILSE IDVDSLDALA RRVVPAVIAD DSDDNGLQAL
PDAIDEPTAR RRLADLAARN VVARSMIGLG YYDTVTPPVI LRNVVENPAW YTAYTPYQPE
ISQGRLEALL NFQTMVADLT AMQVANASML DEATAAAEAM TLMRRAGRSK SHRLVVDADL
FPQTRAVLET RAEPLGIELV EASLHPDRPD RGLPEGDFFG VVMQVPGASG RIVDAAPIIA
AAHDRGALVA VGADLLALTL ITPPGEQGAD VCFGTTQRFG VPMGFGGPHA GYLAVHTAHA
RQLPGRLVGV SKDADDNLAY RLALQTREQH IRREKATSNI CTAQVLLAVV AAMYASYHGA
DGLRAIARRA HASAAFLADS LTAAGFSVDH STFFDTITVR TPGRADAVIG QAKRDGAVNL
RRVDPDRVGI ACDETTSADD LAAVLRAFSA QGVKPRSFAQ PIETRTTEYL THPAFNRYRT
ETAMLRYLRQ LSDKDIALDR SMIPLGSCTM KLNATTEMEA ITWPGFADLH PFAPAADTAG
IRELIATLED WLVAITGYDR VSLQPNAGSQ GEYAGLLAIR RYHRSRGEED RDICLIPSSA
HGTNAASAVM AGMRVVVVGC RENGDVDVDD LRAKIDKHRD ALAAIMITYP STHGVFEHDI
AEICAAVHDA GGQVYVDGAN LNALVGVARP GRFGGDVSHL NLHKTFCIPH GGGGPGVGPV
AVRSHLAGFL PGHPFADELP DTGAVSAAPY GSASILPITY AYIAMMGADG LRRATLTAIA
SANYIARRLA DHFPVLYTDG TSESTHGVGG FVAHEAILDL RPLTKATGVT VDDVAKRLAD
YGFHAPTMSF PVAGTLMVEP TESENLDELD AFCDAMIAIR AEIDKVAVGE WPLDDNPLRG
APHTAEALVG DWDHPYSREV AVYPQGLPSA GARAKVWPAV RRIDGAFGDR NLVCSCPPID
AFAD
//
