ID A0A3R8QPB5_9FLAO Unreviewed; 952 AA.
AC A0A3R8QPB5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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:RRO16813.1};
GN ORFNames=EIG84_07730 {ECO:0000313|EMBL:RRO16813.1};
OS Flavobacteriaceae bacterium 14752.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=2491711 {ECO:0000313|EMBL:RRO16813.1, ECO:0000313|Proteomes:UP000274596};
RN [1] {ECO:0000313|EMBL:RRO16813.1, ECO:0000313|Proteomes:UP000274596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14752 {ECO:0000313|EMBL:RRO16813.1,
RC ECO:0000313|Proteomes:UP000274596};
RA Yu Y.;
RT "Wangjiella luteus gen. nov., sp. nov., a novel bacterium of the family
RT Flavobacteriaceae isolated from a saline lake.";
RL Submitted (NOV-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:RRO16813.1}.
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DR EMBL; RRZV01000067; RRO16813.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R8QPB5; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000274596; 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}.
FT DOMAIN 8..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 451..728
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 773..890
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 701
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 952 AA; 105642 MW; ACCB4AB0D86E8B98 CRC64;
MNTSVFANRH IGPRGDNFND MLKTIGVSSI EELIFETLPD NIRLKQPLDL PEALSEYQFS
QHINALAEKN QSFKTYIGLG YHEAILPAVI QRNILENPGW YTAYTPYQAE IAQGRLEALL
NFQTVVSDLT GMELANASLL DEATAAAEAM SMLFAVRSRT KKKQKAQKFF VSEDIFPQTL
ALLETRAEPQ NIELVVGRHE DFDFAEDYFG AFLQYPGKTG QIHNLKSFVE KAHSLEIKTV
VAADLMSLVL LEAPGSWGVD VVVGTTQRFG IPLGYGGPHA AYYATKEDYK RQIPGRIIGV
TKDMDGNRGL RMALQTREQH IKRDRATSNI CTAQVLLAVM AGMYAVYHGP KGLKFIAEQI
HQKTANLADA IERLGIFQAN DTYFDTLLLK ADAEKIKTIA EKHQINFYYP DAESVCVSIN
ETTSVEDLNA ILKVFKAYKS ANDVVIQQLE NFDIITKHHL NRTTDFLQSS VFNSYHSETE
LMRYIKSLER KDLSLNHSMI SLGSCTMKLN AAAEMLPLSN PKWGNLHPYV PVEQAQGYHE
MLKQLEQYLT EITGFSATSL QPNSGAQGEY AGLMVIRAYH QSRGESHRHI CLVPSSAHGT
NPASAVMAGM KVVVVKSTEK GNIDVEDLKA KAEKYSKDLA ALMVTYPSTH GVFESSIKEI
TDCIHQHGGQ VYMDGANMNA QVGLTSPGAI GADVCHLNLH KTFAIPHGGG GPGVGPICVA
KQLVPFLPSN PLIETGGDKS ISAISAAPWG SALVCIISYA YIRMLGEEGL RRSTETAILN
ANYIKERLKD HYPTLYAGEC GRAAHEMIID CRPFKKNGIE VKDIAKRLID YGFHSPTVSF
PVAGTMMIEP TESESKIELD RFCDAMINIR QEISKCKPED DGNLLTNAPH TQAMLTADEW
QFNYTRQQAA FPLDYVADNK FWPSIRRVDE GYGDRNLICS CNPIEDYMEE AS
//
