ID A0A0Q9ZGT8_9FLAO Unreviewed; 948 AA.
AC A0A0Q9ZGT8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=APR42_07475 {ECO:0000313|EMBL:KRG28606.1};
OS Salegentibacter mishustinae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Salegentibacter.
OX NCBI_TaxID=270918 {ECO:0000313|EMBL:KRG28606.1, ECO:0000313|Proteomes:UP000051643};
RN [1] {ECO:0000313|EMBL:KRG28606.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 12263 {ECO:0000313|EMBL:KRG28606.1};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Salegentibacter mishustinae KCTC 12263.";
RL Submitted (OCT-2015) 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:KRG28606.1}.
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DR EMBL; LKTP01000023; KRG28606.1; -; Genomic_DNA.
DR RefSeq; WP_057482265.1; NZ_QKZW01000001.1.
DR AlphaFoldDB; A0A0Q9ZGT8; -.
DR STRING; 270918.APR42_07475; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000051643; 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:UP000051643}.
FT DOMAIN 9..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 452..729
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 772..888
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 700
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 948 AA; 104666 MW; AADC299DC0EB1AC3 CRC64;
MRTDSFALRH IGPRESNLQA MLDTIGVDSL EQLIYETIPD DIRLKSPLNL PAALSENQYA
EHIGKLAAKN KVFKTYIGLG YHQGILPAVI QRNILENPGW YTAYTPYQAE IAQGRLEALL
NFQTMVSDLT GMEIANASLL DESTAAAEAM GLLFAVRDRK QKKDDVNKFF VSEQALPQTI
DLIKTRADFM GIELVVGNHE EFDFSDKFFG ALVQYPGKFG QVFNYADFVS KCKDAEIKVA
VAADILSLVK LQAPGELGVD VVVGTTQRFG IPLGYGGPHA AYFATKEEYK RNLPGRIIGV
TKDLDGNHAL RMALQTREQH IKRDRATSNI CTAQVLLAVM AGMYAVYHGP DGLKYIADTV
HFSTVTLAEE LEKMGIKQLN SAYFDTLQVK ADAQKIKAEA EKNEINFYYP DAETVCISLN
ETTTQEDINN ILKVFATVSG EKSTEVESLK EESAIPSALQ RKTEFLTHKV FNLYHSETEL
MRYIKNLERK DLSLNQSMIS LGSCTMKLNA ASEMLPLSNP QWGNIHPFVP VEQAEGYQIV
LKRLEDQLTE ITGFSATSLQ PNSGAQGEYA GLMTIRAYHE SRGEGHRNIC LIPSSAHGTN
PASAVMAGMK VVVTKASENG NIDVDDLREK AIKHKDNLAA LMVTYPSTHG VFESAIKEIT
QIIHNNGGQV YMDGANMNAQ VGLTNPGVIG ADVCHLNLHK TFAIPHGGGG PGVGPICVAE
QLKPFLPGNP VIKTGGENAI GAISSAPWGS SLVCLISYGY ITMLGSKGLQ KATEYAILNA
NYIKERLNEH YKTLYSGERG RAAHEMILDC RPFKENGIEV VDIAKRLIDY GFHAPTVSFP
VAGTMMIEPT ESESKAELDR FCDALISIRQ EIEDLDSEED NVLKNAPHTI TMLTSDEWKF
SYTREKAAYP LNYVSENKFW PSVRRVDEAF GDRNLMCTCP PIEEYMDA
//
