ID A0A2U1CM06_9BURK Unreviewed; 964 AA.
AC A0A2U1CM06;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=C7440_1524 {ECO:0000313|EMBL:PVY62035.1};
OS Pusillimonas noertemannii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pusillimonas.
OX NCBI_TaxID=305977 {ECO:0000313|EMBL:PVY62035.1, ECO:0000313|Proteomes:UP000246145};
RN [1] {ECO:0000313|EMBL:PVY62035.1, ECO:0000313|Proteomes:UP000246145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10065 {ECO:0000313|EMBL:PVY62035.1,
RC ECO:0000313|Proteomes:UP000246145};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (APR-2018) 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:PVY62035.1}.
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DR EMBL; QEKO01000002; PVY62035.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1CM06; -.
DR STRING; 1231391.GCA_000308195_01553; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000246145; 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:UP000246145}.
FT DOMAIN 18..440
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 466..743
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 786..907
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 713
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 964 AA; 102337 MW; 1D669DE7E2C7E3EC CRC64;
MAAIPSCTPR ADGEFIARHI GPDASDRARM LDAIGIESLD ALVASVLPDS IALDRPLGLP
GPRSEADVLA ELQGLAGRNR VLRSYIGQGY YGTHVPPVIL RNVLENPAWY TAYTPYQPEI
SQGRLEALLN FQTMVADLAG LDIANASLLD EATAAAEAMA LAWRATASSC PVFFASSHCH
PQTLQVLRTR AEPLGIQLQV GDETAQPLPE CFGVLLQYPH SLGGVVDYRD LISQAHARGA
VVVMATDLLA LALLTPPGEL GADIAVGSAQ RFGVPMAYGG PHAAFMACKD SYKRNLPGRI
VGVSRDAHGA PALRLALQTR EQHIRREKAT SNICTAQVLL AVMAGMYAVW HGPQGITRIA
RRAAAQAGWL RRVLGGMGLK VLNPHGFDTL HVDCGANAGA VMMAALQAGI NLRRVDERSL
AVSLDETVTE DDLAMLAEVF SKGAAAGSSL FEAPAFEPSA GDAADIAIPA ALLRKDGILS
QPVFSRIKSE TDMLRYLRSL ADKDLALDRG MIPLGSCTMK LNASAEMMPI TWPGFCDMHP
YAPADQAQGY QELVERLSAA LCEITGYDAV SLQPNSGAQG EYAGLLAIRA FHRHQGQRQR
DICLIPASAH GTNPASARMA GMQVLVVESD ANGQVDLADL DRKIAQAADR LAALMITYPS
THGVFEPAIT AICDKVHAAG GQVYLDGANM NAMVGLAKPG LFGSDVSHLN LHKTFCIPHG
GGGPGAGPVA VRAHLAPYLP GRIDAHNGLE DAAVGPVSAA THGSAGIMPI PYAYIALMGA
EGLREASRVA ILNANYIAAR LRRHYPLLYA GDDGRVAHEC ILDIRPLTAR TGVSAEDIAK
RLMDYSFHAP TMGFPVPGTL MIEPTESEGL AELDRFIEAM IAIRAEIAAI EEGAAPAQDN
LLSNAPHTAQ ALLAAEWKHG YSREQAAYPV ACLRESKYWP PVGRVDNAWG DRNLVTMASK
DCAG
//
