ID A0A2N3HFI2_9FLAO Unreviewed; 949 AA.
AC A0A2N3HFI2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:PKQ43528.1};
GN ORFNames=CSW08_17820 {ECO:0000313|EMBL:PKQ43528.1};
OS Confluentibacter flavum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Confluentibacter.
OX NCBI_TaxID=1909700 {ECO:0000313|EMBL:PKQ43528.1, ECO:0000313|Proteomes:UP000233435};
RN [1] {ECO:0000313|EMBL:PKQ43528.1, ECO:0000313|Proteomes:UP000233435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3B {ECO:0000313|EMBL:PKQ43528.1,
RC ECO:0000313|Proteomes:UP000233435};
RA Yu L.;
RT "Confluentibacter flavum sp. nov., isolated from the saline lake.";
RL Submitted (DEC-2017) 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:PKQ43528.1}.
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DR EMBL; PJEO01000057; PKQ43528.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3HFI2; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000233435; 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:UP000233435}.
FT DOMAIN 9..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 472..729
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 772..889
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 949 AA; 104541 MW; 69E82410A09CA2F3 CRC64;
MNTNAFALRH IGPNENDQIQ MLKTIGVDSL DQLINETVPS DIRLKKALHL DAPMTEHDYL
LHIHELSKKN KAYKTYIGLG YHPTILPAVI QRNILENPGW YTAYTPYQAE IAQGRLEALL
NFQTMITDLT GMEIANASLL DESTAAAEAM SLLFAVRERD QKKAGVNKFF VSENILPQTL
SLLETRAIPI GIKLIVGNEA TFDFSSEFFG AILQYPGKDG QVTDIKTFIS KAQNAQIKVA
VAADILSLIK LEAPGKFGAD VVLGTTQRFG IPMGYGGPHA AYFATKDAYK RDLPGRIIGV
TKDIDGNRAL RMALQTREQH IKRDKATSNI CTAQVLLAVM ASMYAVYHGP KGLKFIADKI
HNKATTLAKA LEKLGYNQIN TSYFDTLQIK TNAKKIKKIA KEKKVNLYYP DSETVTISIN
ETTAIRDINY LISIFAEAAK KETIIISSIT EANNIAEALQ RQSDFLTLDV FNTYHSETEL
MRYIKLLERK DLSLNHSMIS LGSCTMKLNA ASEMLPLSWF KWTNIHPFAP SKQAQGYLTV
LKELEDQLTE ITGFAATSLQ PNSGAQGEFA GLMVIKAYHE SRGDHHRNIC LIPSSAHGTN
PASAVMAGMR VVVTKSTPEG NIDVDDLREK AELHKDNLSC LMVTYPSTHG VYESAIKDIT
KIIHDHGGQV YMDGANMNAQ VGLTNPGNIG ADVCHLNLHK TFAIPHGGGG PGVGPICVAK
QLAPFLPGNP IKKVGGVKAI TAISAAPFGS ALVCLISYGY IKMLGAEGLT QATKIAILNA
NYIKRRLEGY FDTLYSGENG RAAHEMIVDC RAFKVSGIEV TDIAKRLMDY GFHAPTVSFP
VAGTLMIEPT ESESKAEMDR FCDAMISIRK EIDNASKDDD NNVLKNAPHT LEMLTANEWY
FPYSRNTAAY PLDYVKNNKF WPSVRRVDDA YGDRNLICTC APIEVYMEA
//
