ID A0A1I5WXM3_9BACT Unreviewed; 965 AA.
AC A0A1I5WXM3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN04515674_1134 {ECO:0000313|EMBL:SFQ24492.1};
OS Pseudarcicella hirudinis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Pseudarcicella.
OX NCBI_TaxID=1079859 {ECO:0000313|EMBL:SFQ24492.1, ECO:0000313|Proteomes:UP000199306};
RN [1] {ECO:0000313|EMBL:SFQ24492.1, ECO:0000313|Proteomes:UP000199306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E92,LMG 26720,CCM 7988 {ECO:0000313|Proteomes:UP000199306};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
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; FOXH01000013; SFQ24492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5WXM3; -.
DR STRING; 1079859.SAMN04515674_1134; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000199306; 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:UP000199306}.
FT DOMAIN 14..443
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 459..740
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 782..903
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 709
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 965 AA; 105888 MW; D60C40A1AF603F82 CRC64;
MKIDLRYQEK FETRHNNSNE ADIKEMLDLI GADSIETLIA QTVPSAIRLP QELRLPAPKS
EYQFLKDFKK LAQQNVIHKS HIGMGYYDTI VPPVILRNVL ENPAWYTAYT PYQAEIAQGR
LEMLLNYQTM VIELTGMEIA NASLLDEGTA AAEAMTMLYN LRKASKKNAE TFFVSEFCHP
QTIDILITRA TPLGINILVG DHRKIDLTNE DIFGAILQYP ASEGEVFDYT ELIAAAHELN
VNVVVAADLM ALSLLTPPGE MGADVVIGCS QRFGVPMGFG GPHAAFFATK DEFKRHIPGR
IIGVSVDSEG NRALRMALQT REQHIRREKA TSNICTAQVL LSVMAAAYGV YHGPEGIKAI
AKRIYGLTQL TAKALESLGF TVENSQYFDT LKVNTGNHTE AIRAEAIASK INFRYFKDSA
LHLGISLDET CFFEDVVNIV SVFEKISGKS ADLAKIETTI DWAISENLTR KSDFMTHQVF
NNYHSEHEML RYLKSLENKD LSMVHSMISL GSCTMKLNAT TEMIPVTWSE FGSIHPFAPA
GQTLGYKELV TNLNDWLCEI TGFAKMSLQP NSGAQGEYAG LMVIRAYHES RGDSHRNIAL
IPSSAHGTNP ASAVMAGMKV VVTKCDDNGN IDVADLKAKA EQYSENLACL MVTYPSTHGV
FEESIKEICA LIHEHGGQVY MDGANMNAQV GLTSPATIGA DVCHLNLHKT FCIPHGGGGP
GMGPIGVAPQ LVPFLPGHAV VEGVGGEFAI NAVSAAPYGS ASILTISYAY IAMMGGEGLR
KATQTAILNA NYIKARLEND YPVLYTGSQG RCAHEMILDC RPFKLSAGVE AEDIAKRLMD
YGFHAPTLSF PVAGTLMVEP TESESKAELD RFCDAMLAIR QEIREIEEGN ADKASNVLKH
APHTQAVVLT ENWNRPYSRE KAVFPLAYVK ANKFWPAVSR VDSAYGDRNL ICACIPVEEY
AHQEA
//
