ID A0A1M7GKI7_9ACTN Unreviewed; 964 AA.
AC A0A1M7GKI7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=SAMN05216499_1093 {ECO:0000313|EMBL:SHM16770.1};
OS Actinacidiphila paucisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310782 {ECO:0000313|EMBL:SHM16770.1, ECO:0000313|Proteomes:UP000184111};
RN [1] {ECO:0000313|EMBL:SHM16770.1, ECO:0000313|Proteomes:UP000184111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2025 {ECO:0000313|EMBL:SHM16770.1,
RC ECO:0000313|Proteomes:UP000184111};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRBI01000009; SHM16770.1; -; Genomic_DNA.
DR RefSeq; WP_073498511.1; NZ_FRBI01000009.1.
DR AlphaFoldDB; A0A1M7GKI7; -.
DR STRING; 310782.SAMN05216499_1093; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000184111; 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:UP000184111}.
FT DOMAIN 22..450
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 456..739
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 785..906
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 712
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 964 AA; 101806 MW; 2A79A878B562A75B CRC64;
MTEPTARRTP LADLEAGLPF ARRHIGPDAA DRAKMLAQVG YGSLDELTAA AVPDTIRSAE
ALALPAARTE AEVLAELREL ADRNQVLTPM IGLGYYGTFT PPVILRNVME NPAWYTAYTP
YQPEISQGRL EALINFQTVV ADLTGLPTSG ASLLDEATAA AEAMALSRRV GKVKDGVFLV
DADTFPQTTA VIGTRAEPTG VEVVVADLSD GIPAEVAERG VFGVLLQYPG ASGAVRDLRP
VIEQAHGLGA VVTVAADLLA LTLLTSPGAL GADIAVGTTQ RFGVPMGFGG PHAGYMAVRE
SYARNLPGRL VGVSVDADGD TAYRLALQTR EQHIRREKAT SNICTAQVLL AVMAGIYAVY
HGPEGLAQIA RRTHRYAAVL ATGLRAAGVE LVHDGYFDTL TARVPGRAAE VVAAARAAGV
NLRQTDADLV GIACDETTNR AALAAVLAAF GATGDIDDID AATPDALPAG LVRTEPYLTH
PVFHLHRSET AMLRYLRRLA DRDYALDRGM IPLGSCTMKL NATTEMEPVT WPEFGALHPF
APAEQAEGYL TLIRGLEDQL AEVTGYDKVS LQPNAGSQGE LAGLLAVRAY HRAAGDTART
VCLIPSSAHG TNAASAVMAG MRVVVVRTGQ DGDVDIDDLR AKIEQHREQL AVLMVTYPST
HGVFEDNITD ICAAVHDAGG QVYVDGANLN ALVGLARPGR FGADVSHLNL HKTFCIPHGG
GGPGVGPVAV RAHLAPYLPN HPLQPAAGPA TGVGPISAAP WGSAGILPIS WTYVRLMGAD
GLRQATQQAV LSANYVARRL EPHYPVLYTG PGGLVAHECI VDLRPLAKET GVSVDDIAKR
LIDYGFHAPT MSFPVAGTLM IEPTESEDLA ELDRFCDAMI AIRGEADRVG SGEWPADDNP
LRGAPHTAAA LGGDWDHPYS RQEAVFPAGV SAADKYWPPV RRIDGAYGDR NLVCSCPPLD
AYDN
//
