ID A0A2T6E770_9GAMM Unreviewed; 953 AA.
AC A0A2T6E770;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=BGP77_08000 {ECO:0000313|EMBL:PTY37198.1};
OS Saccharospirillum sp. MSK14-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Saccharospirillum.
OX NCBI_TaxID=1897632 {ECO:0000313|EMBL:PTY37198.1, ECO:0000313|Proteomes:UP000244044};
RN [1] {ECO:0000313|EMBL:PTY37198.1, ECO:0000313|Proteomes:UP000244044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSK14-1 {ECO:0000313|EMBL:PTY37198.1,
RC ECO:0000313|Proteomes:UP000244044};
RA Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT "Draft genome of Saccharospirillum sp. MSK14-1.";
RL Submitted (AUG-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:PTY37198.1}.
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DR EMBL; MIES01000033; PTY37198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6E770; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000244044; 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: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|HAMAP-Rule:MF_00711,
KW ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000244044}.
FT DOMAIN 21..440
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 478..737
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 709
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 953 AA; 102255 MW; 008221E976C0F81F CRC64;
MTTSLHQKPL TALADAGFAP RHLGPNADDQ TAMLATLGLN SRADLIGQTV PESLRMDGAL
ALDSGRNESE ALAELAQIAS QNKVLTSHIG QGYYGTHIPA AIARNVLENP AWYTAYTPYQ
PEISQGRLEA LLNFQQVVMD LTGLDLANAS LLDEATAAAE AMTLCQRVNR KNKSNQFFVD
ADTHPQTLAV LRTRAHYLNI ELIIAPAETV AQHSPFGALL SYPGSSGAIG DVQAHLEAAK
NAGAVTAVAT DLLALMLLRS PGELGADIAF GSAQRFGVPL GYGGPHAAFF AVRDAHKRQV
PGRIIGVSVD AKGGQALRMA MQTREQHIRR EKATSNICTA QALLANLASF YAVYHGPNGL
RTIAERVHRF TAILAEGLRR NGVDVAEHFF DTLTFNVDAS VHERAVSAGC NLRRFSDGRV
GVSLDETTAA ADVERLFKVL VGDNHGLDLA ELDAAVLASD TPALPSELRR TDDVLSHPVF
NRYHSETELL RYIKRLENRD YSLVHGMIPL GSCTMKLNAA AEMQPVSWPQ FANVHPFAPA
DQASGYQRLV SDLETQLLAI TGYDALSMQP NSGAQGEYAG LLAIRRYHQA NGDDQRTLCL
IPASAHGTNP ASAALMGLDV VIVACDDNGN VDLDDLAVKA EQAGEKLAAC MITYPSTHGV
FEEGLKQLCD TVHRFGGQVY LDGANLNAQV GLMQPGKVGA DVSHLNLHKT FAIPHGGGGP
GMGPIGVKAH LAPYLPGHGE DSDGAVSAAA FGSAGILPIT WMYNRMLGRD GLQASTEVAI
LGANYLAEAL KDDFDVLYRG SNGRVAHECI LDLRPLKAAT GISEEDVAKR LMDYGFHAPT
MSFPVPGTLM VEPTESESKA ELDRFIDAMR GIRAEIAKVE SGEWAADNSP LRHAPHSQAD
LVGEWNRPYP RELGVFPSEA VKSAKFWPAV NRVDNVHGDR NLMCSCPPIE AYQ
//
