ID A0A0D6NNK7_9PROT Unreviewed; 976 AA.
AC A0A0D6NNK7; A0A6N3T112;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=Abor_065_010 {ECO:0000313|EMBL:GAN67193.1};
OS Acetobacter orientalis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=146474 {ECO:0000313|EMBL:GAN67193.1, ECO:0000313|Proteomes:UP000032670};
RN [1] {ECO:0000313|EMBL:GAN67193.1, ECO:0000313|Proteomes:UP000032670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21F-2 {ECO:0000313|EMBL:GAN67193.1,
RC ECO:0000313|Proteomes:UP000032670};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acetobacter orientalis 21F-2.";
RL Submitted (NOV-2012) 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:GAN67193.1}.
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DR EMBL; BAMX01000055; GAN67193.1; -; Genomic_DNA.
DR RefSeq; WP_048842303.1; NZ_BJVV01000011.1.
DR AlphaFoldDB; A0A0D6NNK7; -.
DR STRING; 1231341.Abor_065_010; -.
DR GeneID; 76205333; -.
DR Proteomes; UP000032670; 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:UP000032670}.
FT DOMAIN 35..457
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 494..752
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 796..917
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 724
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 976 AA; 103476 MW; FA0A51F34DC716E3 CRC64;
MFSLASGSAH SSGCSVDTLP VFAGLKPEAG TFVPRHIGPS ADDVASMLAT VGAPSLDALM
RETLPEAIRA TKPMGIGPGW SEVDVLAHLR TLASQNEVMT SLIGQGYYGT VLPAVIQRNI
LENPAWYTAY TPYQPEISQG RLEALLNFQT MITELTGLDI ANASLLDEAT AAAEAMAMAH
RVAKSKATAF FVDAECHPQT LAVLKTRAEP LGIALVVGCP QTDLVAADVF GALFQYPGTT
GTVADPRTAI DALHAAGAIA VMAADPLALT VLASPGELGA DIAIGSTQRF GVPMGFGGPH
AAYMAVRDAW KRNLPGRLVG VSVDSQGRPA YRLALQTREQ HIRREKATSN ICTAQVLLAV
IAGMYAVYHG PDGLAAIAKR VHGLTTALAA GLKALGVTVE TEHFFDTLTV QVGAGAADIL
ARARSAGINL RNAGHGRLGI SLDETTTPAT IVAVWGAFCT EQSRVEAMAK TLAPAPSALP
ASLVRQSAFL TQPVFRSCQS ETDMLRYLRR LADKDLALDR TMIPLGSCTM KLNATVEMLP
ITWPGFCDMH PFAPIEQTKG YQALFADLEQ WLCAISGYDA VSFQPNSGAQ GEYAGLLAIS
AYHRANGQTN RTVCLIPASA HGTNPASAQM AGMKVVVVKC DAGGNIDLED MRAKVATHAQ
DLSAVMITYP STHGVFEESM REICDLVHQA GGQVYVDGAN MNAQVGLARP ADYGGDVSHF
NLHKTFCIPH GGGGPGMGPI GVRAHLKPFL PGNPAAEGTA QGTTLAVSAA PYGSASILPI
SWAYIRLMGD DGLQRATEVA ILNANYIVSR LAGAYPVLYR GAKGRVAHEC ILDLRPIKDS
VGVTVDDMAK RLVDYGFHAP TVSFPVAGTF MIEPTESEGK AELDRFCDAM LAMREEVRAI
EAGKLTAEHS ALRHAPHTGS MVTATDWHYA YTRQEASFPP GVNPSRKYWP TVSRIDNAHG
DRNLVCSCPD IAEWME
//
