ID A0A1F1QID1_9PSED Unreviewed; 956 AA.
AC A0A1F1QID1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=HMPREF3173_03970 {ECO:0000313|EMBL:OFS76473.1};
OS Pseudomonas sp. HMSC08G10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1581141 {ECO:0000313|EMBL:OFS76473.1, ECO:0000313|Proteomes:UP000179079};
RN [1] {ECO:0000313|EMBL:OFS76473.1, ECO:0000313|Proteomes:UP000179079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC08G10 {ECO:0000313|EMBL:OFS76473.1,
RC ECO:0000313|Proteomes:UP000179079};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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:OFS76473.1}.
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DR EMBL; LWMZ01000016; OFS76473.1; -; Genomic_DNA.
DR RefSeq; WP_070571629.1; NZ_KV793292.1.
DR AlphaFoldDB; A0A1F1QID1; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000179079; 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; 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}.
FT DOMAIN 17..442
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 479..736
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 776..897
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 956 AA; 102938 MW; 316ECB513C846C68 CRC64;
MSTAPIALGT NNSFIARHIG PSEADIEAML ALTGHGSLEA LIDSVIPNSI KGTSVLELTP
GQGESEALAA IKAIAAKNQL FRNHIGQGYY PCHTPAPILR NLLENPAWYT AYTPYQPEIS
QGRLEALLNF QTLIVDLTGM EIANASLLDE ATAAAEAMTF CKRLATNKAP AFFVSNACHR
QTLDVVRTRA EPLGIEVVVG DETHLQGQNL EGYFGLLLQY PASTGAIGDH RALVARAHAA
GALVAVATDL LALTLLTPPG EFGADVVFGS AQRFGVPLGF GGPHAAFFAT RDAFKRDMPG
RLVGLSIDRF GKPALRLAMQ TREQHIRREK ATSNICTAQV LLANIASMYA VYHGPEGLTQ
IARRVHRLTS ILAQGLRQLG HSVEQSHFFD TVSVVTARPV GEVLAAANAQ RLNLRPIDSA
RVGLSLDETC EQQSVEALWQ VFAAPGQALP DFAALAASGV DCLPTPLLRQ SAFLQHEVFN
RYHCETELMR YLRRLADKDL ALDRSMIALG SCTMKLNAAS EMMPITWPEF GALHPFAPAE
QAQGYRQLTD ELEAMLCAAT GYDAMSLQPN AGSQGEYAGL LAIRAYHASR GESGRDVCLI
PSSAHGTNPA TAQMAGMRVV VVNCDARGNV DVADLQSKAE QHKEHLAALM ITYPSTHGVF
EDGITRICEI IHAHGGQVYL DGANMNAMVG LCAPGKFGGD VSHLNLHKTF CIPHGGGGPG
VGPIGVKAHL APFLPGHGHM ARKDGAVSAA PYGSASILPI TWMYIRMMGG EGLKRASQVA
ILSANYIARR LEEHYPVLYT GENGLVAHEC ILDLRPLKDS SGISVEDVAK RLIDFGFHAP
TMSFPVAGTL MVEPTESESK DELDRFCEAM IRIREEIRAV ENGTLDTHDN PLKNAPHTAA
ELAGEWGHGY SRELAVYPQD SLRDNKYWPP VGRVDNVYGD RNLACACPPM SIYQDA
//
