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Database: UniProt
Entry: A0A0L0AWB9_9ENTR
LinkDB: A0A0L0AWB9_9ENTR
Original site: A0A0L0AWB9_9ENTR 
ID   A0A0L0AWB9_9ENTR        Unreviewed;       957 AA.
AC   A0A0L0AWB9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 54.
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=AC791_01355 {ECO:0000313|EMBL:KNC12016.1};
OS   Klebsiella sp. RIT-PI-d.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=1681196 {ECO:0000313|EMBL:KNC12016.1, ECO:0000313|Proteomes:UP000053401};
RN   [1] {ECO:0000313|Proteomes:UP000053401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIT-PI-d {ECO:0000313|Proteomes:UP000053401};
RA   Tan N.E.H., Lee Y.P., Gan H.M., Savka M.A.;
RT   "Whole genome sequencing of endophytes isolated from poison ivy
RT   (Toxicodendron radicans).";
RL   Submitted (JUL-2015) 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:KNC12016.1}.
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DR   EMBL; LGIT01000003; KNC12016.1; -; Genomic_DNA.
DR   RefSeq; WP_049838692.1; NZ_LGIT01000003.1.
DR   AlphaFoldDB; A0A0L0AWB9; -.
DR   STRING; 1681196.AC791_01355; -.
DR   PATRIC; fig|1681196.3.peg.2440; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000053401; 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; 1.
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:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 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|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_00711}; Reference proteome {ECO:0000313|Proteomes:UP000053401}.
FT   DOMAIN          16..440
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          474..739
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          781..902
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   MOD_RES         708
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT                   ECO:0000256|PIRSR:PIRSR603437-50"
SQ   SEQUENCE   957 AA;  104596 MW;  DF5BB1F1B9522C89 CRC64;
     MTQTLSQLEN SGAFIERHIG PDAAQQQAML NTVGAASLDA LIGQIVPKDI QLATPPQVGE
     AATEYAALAE LKNIARRNKR FTSYIGMGYT AVQLPPVILR NMLENPGWYT AYTPYQPEVS
     QGRLEALLNF QQVTLDLTGL DMASASLLDE ATAAAEAMAM AKRISKLKNA NRFFVAADVH
     PQTLDVVRTR AETFGFDVIV DDADKVLDHQ DVFGVLLQQV GTTGEIHDYS ALTAELKTRK
     IVVSVAADFM TLVLLTAPGK QGADIVFGSA QRFGVPMGYG GPHAAFFAAK DEFKRSMPGR
     IIGVSKDAAG NTALRMAMQT REQHIRREKA NSNICTSQVL LANIASLYAV YHGPVGLKRI
     ASRIHRLTDI LAAGLQQKGL KLRHAHYFDT LCVDVADKAA VLARAEAAEI NLRSDIHNAV
     GMTLDESTTR ENVLALFNVL LGDDHGLDID ALDKDVAHDS RAIPAAMLRD DDILSHPVFN
     RYHSETEMMR YMHSLERKDL ALNQAMIPLG SCTMKLNAAA EMIPITWPEF AELHPFCPAD
     QAEGYHQMIN QLSDWLVKLT GYDALCMQPN SGAQGEYAGL LAIRHYHESR NEGHRDICLI
     PSSAHGTNPA SAQMAGMRVV VVSCDKNGNI DLNDLRAKAE HSSENLSCIM VTYPSTHGVY
     EETIREVCEI VHHFGGQVYL DGANMNAQVG ITSPGFIGAD VSHLNLHKTF CIPHGGGGPG
     MGPIGVKAHL APFVPGHSVV QIEGMLTRQG AVSAAPFGSA SILPISWMYI RMMGAQGLKQ
     ASQVAILNAN YIASRLKEAF PVLYTGRDGR VAHECILDIR PLKEASGISE LDIAKRLIDY
     GFHAPTMSFP VAGTLMVEPT ESESQMELER FIEAMLSIRA EIDRVQNGEW TLEDNPLVNA
     PHTQYELAAE WTHGYSREEA VFPAGSVNKY WPTVKRLDDV YGDRNLFCSC VPLSEYQ
//
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