ID A0A501WCB4_9GAMM Unreviewed; 952 AA.
AC A0A501WCB4;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 18-JUN-2025, entry version 24.
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 ECO:0000313|EMBL:TPE47249.1};
GN ORFNames=FJM67_14745 {ECO:0000313|EMBL:TPE47249.1};
OS Maribrevibacterium harenarium.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Oceanospirillales; Oceanospirillaceae; Maribrevibacterium.
OX NCBI_TaxID=2589817 {ECO:0000313|EMBL:TPE47249.1, ECO:0000313|Proteomes:UP000315901};
RN [1] {ECO:0000313|EMBL:TPE47249.1, ECO:0000313|Proteomes:UP000315901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB171799 {ECO:0000313|EMBL:TPE47249.1,
RC ECO:0000313|Proteomes:UP000315901};
RA Huang H., Mo K., Hu Y.;
RT "A novel bacterium of genus Marinomonas, isolated from coastal sand.";
RL Submitted (JUN-2019) 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=N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein]
CC + glycine + H(+) = N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-
CC [glycine-cleavage complex H protein] + CO2; 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:ARBA00049026, 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:TPE47249.1}.
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DR EMBL; VFRR01000044; TPE47249.1; -; Genomic_DNA.
DR RefSeq; WP_140590885.1; NZ_VFRR01000044.1.
DR AlphaFoldDB; A0A501WCB4; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000315901; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:TreeGrafter.
DR GO; GO:0016594; F:glycine binding; IEA:TreeGrafter.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:TreeGrafter.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR CDD; cd00613; GDC-P; 2.
DR FunFam; 3.40.640.10:FF:000005; Glycine dehydrogenase (decarboxylating), mitochondrial; 1.
DR FunFam; 3.40.640.10:FF:000007; glycine dehydrogenase (Decarboxylating), mitochondrial; 1.
DR FunFam; 3.90.1150.10:FF:000007; Glycine dehydrogenase (decarboxylating), mitochondrial; 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 NCBIfam; NF003346; PRK04366.1; 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:UP000315901}.
FT DOMAIN 17..437
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 469..731
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 773..894
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 700
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 952 AA; 103707 MW; 603E3AC770050A46 CRC64;
MTSRIRDLLG DNEFISRHIG PDDNDRQQML AAIGSNTLTE LIEKTVPEAI RNMPLDFSNQ
AVSENEALSQ LRAIAAKNRV ARSFIGMGYH DTHVPTPVLR NLLENPGWYT AYTPYQPEIS
QGRLEALLNF QQVVIDLTGM EISNASLLDE ATAAAEAMTL MQRSSKKKNT TLFVSDNCLP
QSIDVIKTRA ELLEIDVVVA PLADLDKHDV FGVITQYPGI DGQVVDLTDF IAKAHAQDAL
VTLSADLMAL CLIKSPGEMG ADIVVGSAQR FGVPMGFGGP HAAFLATKDK FKRSMPGRVI
GVSVDSHGKP ALRMAMQTRE QHIRREKATS NICTAQALLA MMAGFYAVYH GPKGLRKIAS
RIAGFTSIIA EKVGSTFEVN STHFDTLVIK TNDQTQVIFD AAKQKGINLF KVNSKTLSLS
VSETTTLTDI VDLLASFNIL LTEQEIADSA ADLGIPAAML RTDEYLTHPV FNTHHSETEL
MRYMHQLEVK DIALNQSMIP LGSCTMKLNA AAEMIPVTWA EFSNIHPFAP LDQVQGYQQL
LDDLIAMLSK ATGYDTISLQ PNSGAQGEYA GLIAIDKYHK SRGDHNRDVC LIPSSAHGTN
PASAALAGMK VVIVKCDENG NIDLDDLKAK AAQHADKLSC IMVTYPSTHG VFEEHIREVC
QVVHDHGGQV YIDGANLNAL VGIAPPGLFG GDVSHLNLHK TFCIPHGGGG PGMGPIGVKS
HLGPFLPGHS VSPVVQQSVQ HGAVSAAPYG SANILVITWM YIKMMGDQGL RDATANAILN
ANYIATRLAG HYPVLYTGKN DTVAHECIID IRPIKAESGI SEEDIAKRLM DFGFHAPTMS
FPVAGTLMIE PTESESKEEL DRFCDAMIQI KAEINKVQAG EWPLEDNPLV NAPHTAASLM
AAEWNHAYSR EEAAYPLPWI RARKYWPPVG RIDNVYGDRN LYCECPPIES YL
//
