ID G6XKH2_9PROT Unreviewed; 948 AA.
AC G6XKH2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=GMO_19880 {ECO:0000313|EMBL:EHH67768.1};
OS Gluconobacter morbifer G707.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=1088869 {ECO:0000313|EMBL:EHH67768.1, ECO:0000313|Proteomes:UP000004949};
RN [1] {ECO:0000313|EMBL:EHH67768.1, ECO:0000313|Proteomes:UP000004949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G707 {ECO:0000313|EMBL:EHH67768.1,
RC ECO:0000313|Proteomes:UP000004949};
RA Lee W.-J., Kim E.-K.;
RT "Genome sequence of Gluconobacter morbifer G707, isolated from Drosophila
RT gut.";
RL Submitted (OCT-2011) 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:EHH67768.1}.
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DR EMBL; AGQV01000006; EHH67768.1; -; Genomic_DNA.
DR RefSeq; WP_008852135.1; NZ_AGQV01000006.1.
DR AlphaFoldDB; G6XKH2; -.
DR STRING; 1088869.GMO_19880; -.
DR PATRIC; fig|1088869.3.peg.1982; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000004949; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004949}.
FT DOMAIN 18..441
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 479..735
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 769..890
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 706
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 948 AA; 101923 MW; 571909F34374BC17 CRC64;
MTAVTILWPE QTEAFSSRHI GPRPADIHEM LRTVRASSLE DLIDRTIPDA ILDRGDHGIG
PALTEQEALT RLRGIASRNR VLTSMIGQGY YDTILPPVIQ RNILENPAWY TAYTPYQPEI
SQGRLEALLN FQTLVADLTG LDIANASLLD EGTACAEAMA LAKRVGKAKS NRFFVDADTH
PQTIDVVRTR AEPLGWEIVV GDPETDLDAS SVFGALLSYP GSSGAVRDPR RIITALHDHG
AIAAVTCDPL AMVLLESPGA LGADIAIGSM QRFGVPMGGG GPHAGFMATR DAYKRNMPGR
LVGVSRDSAG HPAYRLALQT REQHIRREKA TSNICTAQVL LAVIASMYAV YHGPEGLRAI
AERVHGMASI LAEGLKALGL SVETDAFFDT ITVNAGVDAA SVMERALAAG INLRDAGQGR
IGISCDETTA PDTIIAVWKA FCPEDGRVSV LERDLAVTER LPAGLRRSAD LLTHPVFHAH
RSETDLLRYM RALSDKDLAL DRTMIPLGSC TMKLNATAEM IPITWPEFAR MHPFAPADQQ
QGYAELFAYL ERTLCAISGY DAVSLQPNSG AQGEYAGLLA IRGYHRARGD GERDVCLIPA
SAHGTNPASA QMAGMRVAVV ACDENGNVDV EDLKTKIARH DGQIAAIMIT YPSTHGVFEE
RIVEICDLVH AAGGQVYLDG ANLNAQVGLA RPGLYGADVS HFNLHKTFCI PHGGGGPGMG
PIGVREHLRP YLPGRNGVAV SAAPYGSASI LPISAAYIMM MGDAGLRRAT ELAILNANYI
AARLEGHYPV LYRGANGFTA HECIVDLRPL KDAVGVTVDD IAKRLIDHGF HAPTVSFPVA
GTFMIEPTES EGKGELDRFC EAMIAIRQEI AAVEGGDIGM EDSPLRFAPH TTADLVGDWE
RRYSREAGCF PGGVNTSKYW SPVGRLDNAW GDRNLICSCP DMSSYAED
//
