ID A0A495EBH4_9FLAO Unreviewed; 949 AA.
AC A0A495EBH4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=CLV91_0120 {ECO:0000313|EMBL:RKR14051.1};
OS Maribacter vaceletii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=1206816 {ECO:0000313|EMBL:RKR14051.1, ECO:0000313|Proteomes:UP000269412};
RN [1] {ECO:0000313|EMBL:RKR14051.1, ECO:0000313|Proteomes:UP000269412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25230 {ECO:0000313|EMBL:RKR14051.1,
RC ECO:0000313|Proteomes:UP000269412};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (OCT-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:RKR14051.1}.
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DR EMBL; RBIQ01000007; RKR14051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495EBH4; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000269412; 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:UP000269412}.
FT DOMAIN 9..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 466..727
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 773..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; 104635 MW; 62F95684AE3D5E20 CRC64;
MRTDLFASRH IGIKKEDYKH MLQSIGVANL EQLIYETIPD DIRLKQDLQL SPAMSEHEFL
NHLEALSNKN KVFKSYIGLG YHESLIPSVI KRNILENPGW YTAYTPYQAE IAQGRLEALL
NFQTVVCDLT AMEIANASLL DESTAAAEAM TMLFDVRSRA QKKANILKFF VSEEVLPQTL
SLLQTRSTPL GIELVIGNHE EFTFTNDFFG VLLQYPGKYG QVHNFDSFVS KANENDIKVA
VAADILSLTL LKPPGEFGVD VVVGTTQRFG IPLGYGGPHA AFFATKEAYK RNIPGRIIGI
TKDTDGKQAL RMALQTREQH IKRDKATSNI CTAQVLLAVM AGMYAVYHGP EGLKYIANKI
HAAAVTLATN LEQLGYKQLN TSFFDTITIK AESAVIKPLA EQKEINFYYI DANTISISLN
ESVSVADVET IATIFSEAKE NKTIQITSFT DKKEIDQELQ RSSTFLENPV FNSYHSETEL
MRYIKKLERK DLALNHSMIS LGSCTMKLNA ATQMLPLSSN QWGNVHPFAP VEQAEGYQIV
LKELENDLST ITGFAATSLQ PNSGAQGEYA GLMAIRAYHE SNGDTNRNIC IIPASAHGTN
PASAVMAGMK VIVSKTDERG NIDVADLEEK VKLHSENLSA LMVTYPSTHG VFESSIKQIT
KLIHDHGGQV YMDGANMNAQ VGLTNPATIG ADVCHLNLHK TFAIPHGGGG PGVGPICVAK
QLVPFLPSNP VIKTGGSKAI TAISGAPWGS SLVCLISYSY IKMLGEKGLK QSTITAILNA
NYIKSRLSSG FDVLYTGEKG RAAHEMIIDC RPFKQNGIEV TDIAKRLMDY GFHAPTVSFP
VAGTLMIEPT ESESLPELDR FCDAMLSIRQ EIEEAYSENK DNVLKNAPHT LEMVTNDNWN
FEYSRQKAAF PLDFVKENKF WPSVRRVDDA YGDRNLICSC IPIEAYAEA
//
