ID A0A1E7Q5G4_9GAMM Unreviewed; 963 AA.
AC A0A1E7Q5G4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BI198_07280 {ECO:0000313|EMBL:OEY69387.1};
OS Rheinheimera salexigens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=1628148 {ECO:0000313|EMBL:OEY69387.1, ECO:0000313|Proteomes:UP000242258};
RN [1] {ECO:0000313|Proteomes:UP000242258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH87 {ECO:0000313|Proteomes:UP000242258};
RA Wan X., Hou S.;
RL Submitted (SEP-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:OEY69387.1}.
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DR EMBL; MKEK01000001; OEY69387.1; -; Genomic_DNA.
DR RefSeq; WP_070048953.1; NZ_MKEK01000001.1.
DR AlphaFoldDB; A0A1E7Q5G4; -.
DR STRING; 1628148.BI198_07280; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000242258; 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; IPR018247; EF_Hand_1_Ca_BS.
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.
DR PROSITE; PS00018; EF_HAND_1; 1.
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:UP000242258}.
FT DOMAIN 20..441
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 465..738
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 784..905
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 711
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 963 AA; 104426 MW; 0AA2B0B5F1486476 CRC64;
MTNSAVKTLS QLANHEEFIQ RHIGPDAAET AAMLNELGLD SMEALIAQTV PADIRLPEPL
ATGKARSEVE ALAYLKQAAS KNKMFKSYIG MGYHPTLTPN VILRNVLENP GWYTAYTPYQ
PEIAQGRLEA LLNFQQVTLD ITGMELASAS LLDEATAAAE AMALAKRVGK NKSNYYFIAD
DVHPQTIDVV KTRAEMFGFD IIIGKAADAT NHDVFGALIQ YPTTNGDVRD DSALIAALQA
KKAVVAVATD PMALMLLKSP GQLGADVVLG SAQRFGVPMA FGGPHAAFFA TRDSYKRSMP
GRIIGVSKDR RGNAGLRMAM QTREQHIRRE KANSNICTAQ VLLANMASFY AVYHGPIGLK
NIAERIHRHA DIFAAGLAAK GVNIVNKHWF DTVTFTVSDR AAVIQRGLDA GVNLRTDVAD
SLSVSFHEAS TAADLAQLFA IVLGDNHGLD VEKLDATIVA DGSNSIPADL LRTDTILGHP
VFNQYHSETE MLRYIKKLEN KDLALNHSMI SLGSCTMKLN ATSEMIPITW PEFASIHPFV
PRDQAQGYYQ MLGELGDWLV NITGYDNISL QPNSGAQGEY AGMVAIRKYH ESRGDAHRNI
CLIPVSAHGT NPATAAMASF DIVLVDCDKS GNIDMADLKA KAAEVGDRLA AIMVTYPSTH
GIFEESIREL CDIVHAHGGQ VYMDGANMNA QVGVTSPGFI GSDVSHLNLH KTFCIPHGGG
GPGMGPIGVK SHLTPFLPNH SVVKIDGTGE QNGAVSAAPF GSAGILPISW MYIAMMGANG
LKQATEFAIL NANYMANKLD PIFPVLYRGT NGRVGHECII DIRQLKDASG ITEMDIAKRL
MDFGYHSPTM SFPVAGTLMI EPTESESKAE LDKFIEAMAT IREEIGKVLS GEWTVDNNPL
VYAPHSMQDV FDPAWDRAYS QQYAAFPVAY IAENKFWPTV SRIDDVYGDR NLMCACPSPE
AYR
//
