ID A0A2N4YHJ3_9RHOB Unreviewed; 946 AA.
AC A0A2N4YHJ3;
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:PLL12796.1};
GN ORFNames=C0V75_12035 {ECO:0000313|EMBL:PLL12796.1};
OS Tabrizicola sp. TH137.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tabrizicola.
OX NCBI_TaxID=2067452 {ECO:0000313|EMBL:PLL12796.1, ECO:0000313|Proteomes:UP000234539};
RN [1] {ECO:0000313|EMBL:PLL12796.1, ECO:0000313|Proteomes:UP000234539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH137 {ECO:0000313|EMBL:PLL12796.1,
RC ECO:0000313|Proteomes:UP000234539};
RA Cai h.;
RT "genomes of bacteria within cyanobacterial aggregates.";
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:PLL12796.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PKRQ01000003; PLL12796.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4YHJ3; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000234539; 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:UP000234539}.
FT DOMAIN 16..438
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 468..726
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 765..885
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 697
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 946 AA; 102222 MW; 59D44A1DB376DF08 CRC64;
MSYTPVDYNP YDFANRRHIG PSPAEMAEML KVVGVKTLDE LIDQTVPASI RQKVALGWAP
LSEHALLARM REVGAKNKVM TSLIGQGYYG TVTPPAIQRN ILENPAWYTA YTPYQPEIAQ
GRLEALLNYQ TMIADLTGLP VANASLLDEA TAAAEAMAMA ERVAKSKARG FFVDHGCHPQ
TIAVIKTRAV PLGIEVIVGD PAKMVAEQVF GAIFQYPGTY GHVIDFTKEI AALHAAKAVA
IVATDLLALT ILKEPGAMGA DIAIGSSQRF GVPLGYGGPH AAFMSCKDDY KRAMPGRIVG
VSIDARGNKA YRLSLQTREQ HIRREKATSN VCTAQALLAV MASFYAVFHG PKGLRAIAER
VHFLTNRLAR ALKAAGAKVS PKAFFDTITV EVGVGQAGIL AAARHEGLNF RKIGTDRVGI
SLDETTDEKV LIRVLRAFGI EGVPPHRASL GFPEDMVRQT EYLTHPVFHM NRAESEMMRY
MRRLSDRDLA LDRAMIPLGS CTMKLNAAAE MMPITWPEFG TLHPFAPADQ AAGYREAIAD
LTEKLCEVTG YDAFSMQPNS GAQGEYAGLL TIQAYHRARG EGHRNICLIP VSAHGTNPAS
AQMAGMQVVV VKSAPNGDVD LEDFRQRAEE AGENLAACMI TYPSTHGVFE ETVREICKIT
HDHGGQVYLD GANMNALVGL VKPGEIGSDV SHLNLHKTFA IPHGGGGPGM GPIGVKAHLA
PYLPGHPEGA QGEGPVSAAP YGSASILLIS WAYCLMMGGE GLTQATRVAI LNANYIAARL
KGAYPILFMG NKGRVAHECI LDTRPFADVG VTVDDIAKRL IDNGFHAPTM SWPVAGTLMV
EPTESETKAE IDRFITALMA IRAEIEAVEK GEISAEDSPL RHAPHTVEDL VADWTRKYPR
EQGCFPPGAF RVDKYWPPVG RVDNVHGDRN LICICPPVES YAQAAE
//
