ID C3J9K0_POREA Unreviewed; 963 AA.
AC C3J9K0;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
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:EEN83130.1};
GN ORFNames=POREN0001_0751 {ECO:0000313|EMBL:EEN83130.1};
OS Porphyromonas endodontalis (strain ATCC 35406 / BCRC 14492 / JCM 8526 /
OS NCTC 13058 / HG 370).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=553175 {ECO:0000313|EMBL:EEN83130.1, ECO:0000313|Proteomes:UP000004295};
RN [1] {ECO:0000313|EMBL:EEN83130.1, ECO:0000313|Proteomes:UP000004295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35406 / BCRC 14492 / JCM 8526 / NCTC 13058 / HG 370
RC {ECO:0000313|Proteomes:UP000004295};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (APR-2009) 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}.
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:EEN83130.1}.
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DR EMBL; ACNN01000014; EEN83130.1; -; Genomic_DNA.
DR RefSeq; WP_004333121.1; NZ_ACNN01000014.1.
DR AlphaFoldDB; C3J9K0; -.
DR STRING; 553175.POREN0001_0751; -.
DR GeneID; 84819183; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR Proteomes; UP000004295; 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; 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 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,
KW ECO:0000313|EMBL:EEN83130.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000004295}.
FT DOMAIN 9..436
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 477..740
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 775..896
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 706
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 963 AA; 106828 MW; CBF8562CCA0646EF CRC64;
MDTNKFSTRH MGISDKDLPE MLAAVGVKSV DELMHQVYPE NIFLKEQIDI PEAMTERELA
EHLAELASKN KPFTSYIGQG WYDTVTPAPI QRNVLENPVW YTSYTPYQAE VSQGRLEALF
NFQTVISELT SLPLTNCSLL DEATAGAETA MLLFNERSRA QVKAGANTIF VDKRVFETTQ
AVIRTRVEPQ GMKLVVGDYQ TLEFTPDIFG VIIQYPDSVG AINNYEDFVA KAKANGSTVA
VAADLMSLVM LTPPGEWGAD VVFGSAQRFG IPMYFGGPSA GYLACRMEYK REIPGRIIGI
SKDAYGHPAY RLALQTREQH IKREKATSNI CTAQALLATM SGFYAVYHGA EGLRNIARRI
HSYAGYLAAM LEKLGYKQYN KDYFDTLIIG LPEGVSMERL REVALDCRIN LRYFTCCTCV
GISIDETTLP SDLGVLGYVF AEAAGKEAPE VDNVPQDTLY VDKKWQRTSD FLQHEVFNSY
HTETELMRYI KRLDRKDISL AHSMISLGSC TMKLNAASEL FALSNPYFAN IHPYAPEDQV
EGYTEMLDNL AEYLAKITGF DATSLQPNSG ASGEYTGLRT IRTYLESIGQ GHRDVVILPA
SAHGTNPASA VQCGYKTVIV KTDERGNVDW DDFMVQTEAH KDQIAAMMIT YPSTHGIFET
NIIDLCQRIH DCGGQVYMDG ANMNAQVGYT NPGFIGADVC HLNLHKTFAI PHGGGGPGVG
PICVRAHLAP HLPKHVVRFG DGSNQVSAAP YGSAGVQVIT YSYIRLLGIE GLREATAIAI
LNANYMASRF KDTYGIVYTG ATGRVGHELI LECRKVKEET GVDENDIAKR LMDFGYHAPT
LSFPVHGTLM VEPTESESKA ELDRFCEVMD CIYQEAQEIA QGKADKEDNV LKNAPHPQYE
IVADEWKHSY SRQKAAFALP FLQDNKFWIN VARVDNGYGD RNLVPTMCAC NEFFAKLKEE
QGK
//
