ID A0A2T5C1A5_9BACT Unreviewed; 954 AA.
AC A0A2T5C1A5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=C8N47_109127 {ECO:0000313|EMBL:PTN08391.1};
OS Mangrovibacterium marinum.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Mangrovibacterium.
OX NCBI_TaxID=1639118 {ECO:0000313|EMBL:PTN08391.1, ECO:0000313|Proteomes:UP000243525};
RN [1] {ECO:0000313|EMBL:PTN08391.1, ECO:0000313|Proteomes:UP000243525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28823 {ECO:0000313|EMBL:PTN08391.1,
RC ECO:0000313|Proteomes:UP000243525};
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 (APR-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:PTN08391.1}.
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DR EMBL; QAAD01000009; PTN08391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5C1A5; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000243525; 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:UP000243525}.
FT DOMAIN 9..439
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 471..731
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 775..896
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 704
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 954 AA; 105592 MW; DC7D02E8BA0A2D04 CRC64;
MANDKFVARH IGPRESDITA MLTQLGVSSV QELIDQTVPA NIRLEKPLRL EDGLTERQYY
RKVLALAKKN KVFNTYIGMG YYDTITPAVI LRNVLENPVW YTSYTPYQAE ISQGRLEALL
NFQTMICEMT AMDLANASLL DEATAAAEAM IMILNSRSRA QVKAGANVVL VDRNMWPQTL
DVLHTRAVPL GIELTIGELQ DFSFNEQVIG LMVQYPNANG EVVSYAEITE QAHQQGAKVA
VATDLMSLAL LTAPGEWGAD IVFGNSQRFG VPMGYGGPHA AFFAARDAFK RSLPGRIIGV
SKDVHGNRAL RMALQTREQH IKRERATSNI CTAQALLATM AGFYAVYHGS TGIRQIAERI
HRIAVLLDKE ITALGYTQKN EYYFDTIRFA LPKHVKVEDI EWLSLELEMN FRYFDNGEVG
LSIDETTNLD DINWIIEVFA KAANKRYPTI REYPQEDKLV ESLTRSSAFL TQEVFEKYRS
ETEMVRYIKK LEHRDISLTH SMIPLGSCTM KLNAATEMLP LSWIEFGGIH PFVPKNQARG
YQEMMEELRR DLSEITGFAD VSLQPNSGAA GEYAGLMVIR EYHLSRGDQQ RNVVLIPASA
HGTNPASAVM AGMQVVVVPC DELGNVDVEA LRQKAEEYQD SLSAFMVTYP STHGVFEASI
VEMCAIIHQY GGQVYMDGAN MNAQVGLTNP KRIGADVCHL NLHKTFAIPH GGGGPGVGPI
AVAEHLVDFL PSHPVMNNGH VGISAVSAAP WGSASVLPIT YGYIKMLGAD GLTKATEMAI
LNANYIASAL ADTYGILYTG ENGRVAHEMI LECRHFKGTS GITEADIAKR LMDYGFHAPT
LSFPVHGTLM VEPTESESKQ ELDRFIEALL AIYQEIQAIV DGESDQLNNP LKNAPHTADS
VTSDEWAHPY SRQTAAFPLA WLKENKYWPP VGRIDDAYGD RNLVCTCAPI ETYQ
//
