ID A0A1M6HHH0_9BACE Unreviewed; 949 AA.
AC A0A1M6HHH0;
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=SAMN05444350_11872 {ECO:0000313|EMBL:SHJ21637.1};
OS Bacteroides stercorirosoris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=871324 {ECO:0000313|EMBL:SHJ21637.1, ECO:0000313|Proteomes:UP000184192};
RN [1] {ECO:0000313|EMBL:SHJ21637.1, ECO:0000313|Proteomes:UP000184192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26884 {ECO:0000313|EMBL:SHJ21637.1,
RC ECO:0000313|Proteomes:UP000184192};
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; FQZN01000018; SHJ21637.1; -; Genomic_DNA.
DR RefSeq; WP_025833001.1; NZ_FQZN01000018.1.
DR AlphaFoldDB; A0A1M6HHH0; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR Proteomes; UP000184192; 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}.
FT DOMAIN 9..439
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 472..733
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 772..893
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 949 AA; 104672 MW; 58B1542669A8D9D8 CRC64;
MKSDLLACRH IGISEKDEEK MLRKIGVGSL DELIDKTIPA NIRLKEPLAL PAPMTEYEFG
QHITRLACKN KLYTTYIGLG WYNTITPAVI QRNVFENPVW YTSYTPYQTE VSQGRLEALM
NFQTAVCDLT GMPLANCSLL DEATAAAEAV SMMYALRPRD MQKSGANVVF VDESIFPQTL
AVMTTRAIPQ GIQIRTGKYS ELELTPDIFA CILQYPNASG NAEDYRAFVE KAHAANCKVA
VAADILSLAL LTPPGEWGAD IVFGTTQRLG TPMFYGGPSA GYFATRDEYK RNIPGRIIGW
SKDKYGKLCY RMALQTREQH IKREKATSNI CTAQALLATM AGFYAVYHGP EGIHAIAERI
HSIAAYLEKC IKKLGYKQVN DQYFDTLRFV LPDSVSAQQV RTIALSKEVN LRYFDNGDVG
MSIDETTDVS AANVLLSIFA IAAGKDYTKV DDIPVSNTIN KTLKRQSAYL THEVFNKYHT
ETEMMRYIKR LDRMDISLAH SMISLGSCTM KLNAAAEMLP LSRPEFMCMH PLVPEDQAEG
YRELINNLSE ELKVITGFAG VSLQPNSGAA GEYTGLRVIR AYLENIGQGH RNKVLIPASA
HGTNPASAIQ AGFTTVTCAC DAQGNVDMND LRAKAEENKD DLAALMITYP STHGIFETEI
VEICRIIHDC GAQVYMDGAN MNAQVGLTNP GFIGADVCHL NLHKTFASPH GGGGPGVGPI
CVAEHLVPFL PGHPLFGTPV NTVSAAPFGS AGILPITYGY IRMMGTEGLT RATKIAILSA
NYLAACLKDT YGIVYRGATG FVGHEMILEC RKVHEETGIS ENDIAKRLMD YGYHAPTLSF
PVHGTLMIEP TESESLAELD NFVNVMLTIW EEIQEVKEGK ADKEDNVLIN APHPEYEVVA
NNWEHSYTRE KAAYPIESVR ENKFWINVAR VDNTLGDRKL LPTCYGCFE
//
