ID A0A383U084_9FLAO Unreviewed; 957 AA.
AC A0A383U084;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN Name=gcvP {ECO:0000313|EMBL:SZD72910.1};
GN ORFNames=SAMEA104719789_01025 {ECO:0000313|EMBL:SZD72910.1};
OS Candidatus Ornithobacterium hominis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Ornithobacterium.
OX NCBI_TaxID=2497989 {ECO:0000313|EMBL:SZD72910.1, ECO:0000313|Proteomes:UP000262142};
RN [1] {ECO:0000313|EMBL:SZD72910.1, ECO:0000313|Proteomes:UP000262142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH-22767 {ECO:0000313|EMBL:SZD72910.1,
RC ECO:0000313|Proteomes:UP000262142};
RG Pathogen Informatics;
RL Submitted (SEP-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}.
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};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC 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}.
CC -!- SIMILARITY: Belongs to the GcvP family.
CC {ECO:0000256|ARBA:ARBA00010756}.
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DR EMBL; UNSC01000004; SZD72910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A383U084; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000262142; Unassembled WGS sequence.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SZD72910.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000262142}.
FT DOMAIN 9..436
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 453..734
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 779..899
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT COILED 622..649
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 705
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 957 AA; 106276 MW; C157D7373C4FC8F9 CRC64;
MNTNDFSLRH IGVHGADQEE MLRNIGASSI DQLINEALPE NIRISEDINL PNALTELELS
RHMQALGSLN KIYRSYIGFG YHNTILPPVI QRNILENPGW YTAYTPYQAE IAQGRLQALL
NFQTMVSDLT ALPIANASLL DEGTAAAEAM SMFFSSRTRE QKKNNVNKFF VSDLILPQTL
SVLETKASGL GIEIVTGNHE NIELTSAFFG ALVQYPGKHG ELHDYSDFVE KAHHAEIQVA
MAADILSLVL LRAPGEFGVD AAIGTTQRFG IPMGFGGPHA AYMACQEKYK REIPGRIIGL
SQDSNGKPAL RMALQTREQH IKRQKATSNI CTAQVLLAVM AGMYAVYHGP NGLKYIAETI
HKKAVYLAQV LKELNFEVLD NDFFDTIRVS TKGIDRYQLK SLLESYEINI NFFHPDFVSI
SLDDLDVATD EGFKDLISGF AKYQGVEYKF EMPDTIESKI PKALKRSSDF LTHENFNLYH
TETELMRYIK RLEKKDLALN HSMIPLGSCT MKLNAAAEML PLSKAEFGSI HPFAPQDQTQ
GYLTLINNLE NYLSEITGFA STSLQPNSGA QGEYAGLMVI KEYLKSIGQT QRNVVVIPES
AHGTNPASAV LTGLNVVIVK NLENGEFDIE DLKAKVEKHK NELAALMVTY PSTYGFFDDN
IKEVIKIIHE NGGQVYMDGA NMNAQVGLTN PYNVGADVCH LNLHKTFAIP HGGGGPGVGP
ICVAEHLKEF LPGNPNVNSG SDTEKGLYAI SSAPFGSALI HSISYSYIRL LGSAGLKRST
QFAILNANYL KKRLETAYDV LFTNKNGRVA HEMIIDFRPF KKYGIEVVDI AKRLMDYGFH
APTVSFPVAG TLMIEPTESE SKAELDRFVE ALLEIKKEID EIANGNYPED NNVLKNAPHT
TAILTADKWS FGYSRQKAAY PLEWVRERKF WPSVSRIDDA YGDRNLICTC PPTEDYK
//
