ID V9WLP5_9RHOB Unreviewed; 949 AA.
AC V9WLP5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=Gal_02948 {ECO:0000313|EMBL:AHD10680.1};
OS Phaeobacter gallaeciensis DSM 26640.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1423144 {ECO:0000313|EMBL:AHD10680.1, ECO:0000313|Proteomes:UP000018782};
RN [1] {ECO:0000313|EMBL:AHD10680.1, ECO:0000313|Proteomes:UP000018782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26640 {ECO:0000313|EMBL:AHD10680.1,
RC ECO:0000313|Proteomes:UP000018782};
RA Frank O., Petersen J., Goeker M., Klenk H.-P., Rohde M., Scheuner C.;
RT "Complete genome sequence of the Phaeobacter gallaeciensis type strain CIP
RT 105210T.";
RL Submitted (DEC-2013) 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; CP006966; AHD10680.1; -; Genomic_DNA.
DR RefSeq; WP_024098302.1; NZ_AOQA01000007.1.
DR AlphaFoldDB; V9WLP5; -.
DR GeneID; 31847312; -.
DR KEGG; pgd:Gal_02948; -.
DR PATRIC; fig|1423144.3.peg.2960; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_1_1_5; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000018782; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000018782}.
FT DOMAIN 16..439
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 452..727
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 767..888
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 699
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 949 AA; 103503 MW; EB83AF2788584093 CRC64;
MSFEPTDYLP YDFANRRHIG PSPEEMDDML AVVGAKSLDA LVDDTVPATI RQAAALEFGR
PLSERELLHH MREVAGKNVL KTSLIGQGYH GTVTPPAIQR NILENPAWYT AYTPYQPEIS
QGRLEALLNF QTMISDLTGL EIANASLLDE ATACAEAMTV AQRVSKSKAK AFFVDRDCHP
QNIAVIQTRA APLGIEVIVG NPDKLEADKV FGALFQYPGT YGHVRDFTDH IAQLHVHKAI
GVVAADPLSL TLLKEPGAMG ADIAVGSTQR FGVPVGAGGP HAAYMATKDA YKRAIPGRIV
GVSVDAHGNR AYRLSLQTRE QHIRREKATS NVCTAQALLA VMASMYAVFH GPKGLKAIAQ
RIHRKTVRLA KGLEEAGFKV DPRSFFDTIT VDVGPLQEAV LKSAVDEGLN LRRVGETRVG
ITLDEVTRSE TIEAVWRAFG IRRSDDDFTP EYRVPQNMHR TSDYLTHPIF HMNRAETEMM
RYMRRLADRD LALDRAMIPL GSCTMKLNAA AEMMPLSWPE FANIHPFAPA DQMQGYAEMV
SDLSEKLCQI TGYDAISMQP NSGAQGEYAG LLSIAAYHRA NGQGHRNICL IPMSAHGTNP
ASAQMVGWKV VVVKSADNGD IDLDDFREKA EKHAENLAGC MITYPSTHGV FEETVHEVCQ
ITHDHGGQVY IDGANMNAMV GLSRPGDLGG DVSHLNLHKT FAIPHGGGGP GMGPIGVKAH
LQPHLPGHPE TGGQEGPVSA APFGSASILT ISWAYCLMMG GAGLTQATKV AILNANYIAK
RLEGAYDVLY KGPTGRVAHE CILDTRPFEA SANVTVDDVA KRLIDSGFHA PTMSWPVAGT
LMVEPTESET KAELDRFCEA MLSIREEIRA VEAGEMNAEN NALKNAPHTM EDLVKDWDRP
YSREQGCFPP GAFRVDKYWP PVNRVDNAYG DRHLVCTCPP MEDYAEAAE
//
