ID A0A2I9DZ74_9FLAO Unreviewed; 965 AA.
AC A0A2I9DZ74;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, 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 ECO:0000313|EMBL:GBF20524.1};
GN ORFNames=C21_02696 {ECO:0000313|EMBL:GBF20524.1};
OS Arenibacter sp. NBRC 103722.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Arenibacter.
OX NCBI_TaxID=1113929 {ECO:0000313|EMBL:GBF20524.1, ECO:0000313|Proteomes:UP000095208};
RN [1] {ECO:0000313|EMBL:GBF20524.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-21 {ECO:0000313|EMBL:GBF20524.1};
RA Ito K., Nakajima N., Yamamura S., Tomita M., Suzuki H., Amachi S.;
RT "Draft Genome Sequence of Arenibacter sp. Strain C-21, an Iodine-
RT Accumulating Bacterium Isolated from Surface Marine Sediment.";
RL Genome Announc. 4:e01155-16(2016).
RN [2] {ECO:0000313|EMBL:GBF20524.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C-21 {ECO:0000313|EMBL:GBF20524.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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:GBF20524.1}.
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DR EMBL; BDGL02000012; GBF20524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I9DZ74; -.
DR Proteomes; UP000095208; 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:UP000095208}.
FT DOMAIN 25..451
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 489..745
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 788..905
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 716
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 965 AA; 106165 MW; CE164ED7341AD037 CRC64;
MSNFAHLYFR LKLLEFMRTD LFALRHIGIR EEDLPQMLKT INVNSVDQLI NETIPDDIRI
AKPLALETPM SEHEYLSHIQ VLSEKNKVFK SYIGLGYHES ITPSVIKRNI LENAGWYTAY
TPYQAEIAQG RLEALLNFQT VIAELTGMEL ANASLLDEST AAAEAMTMLF DVRSRDQKKN
NVLKFFVSEE ILPQTLSLLK TRSTPLDIEL IVGKHENFEF GDDYFGALLQ YPGKHGQVHD
YAPFVAKAVE KNIKVAVAAD ILSLALLTPP GEFGADVVVG TTQRFGIPLG YGGPHAAFFA
TKEEYKRSIP GRIIGVTKDT DGKPALRMAL QTREQHIKRD KATSNICTAQ VLLAVMAGMY
AVYHGPKGLK YIANKVHSTA VTLVDSLEKL GLYQTNTSYF DTINIKASSS KVRPIAEKYE
VNFLYVDADT ISIALNEATS LKDLQLIVDI FAEAVGKEAV VINGLLPQSL LENKLVRTST
FLENNVFNSY HSETELMRYI KKLERKDLAL NHSMISLGSC TMKLNAASEM LPLSMARWGN
IHPFVPIDQA EGYQIILKEL EKDLNIITGF TGTSLQPNSG AQGEFAGLMV IRAYHESRGE
GHRNICLIPA SAHGTNPASA VMAGMKVVVT KTDENGNIDV ADLAEKAELH KDNLSALMVT
YPSTHGVFES SIKEITKLIH DNGGQVYMDG ANMNAQVGLT NPATIGADVC HLNLHKTFAI
PHGGGGPGVG PICVAEQLAP FLPGNPVIKT GGDKAITAIS AAPWGSSLVC LISYGYIKML
GENGLTQSTK TAILNANYIK NKLSGKFDVL YTGERGRAAH EMIIDCRPFK ENGIEVTDIA
KRLMDYGFHA PTVSFPVAGT LMIEPTESES LAELDRFCSA MLSIREEIDA ASVEDNNNAL
KNAPHTLEMI TADKWEFPYS RQQAAFPLPY ILENKFWPSV RRVDDTYGDR NLICTCAPIE
AYVEA
//
