ID A0A0N0CZX6_9BACT Unreviewed; 968 AA.
AC A0A0N0CZX6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=AD998_10310 {ECO:0000313|EMBL:KOY88145.1};
OS bacterium 336/3.
OC Bacteria.
OX NCBI_TaxID=1664068 {ECO:0000313|EMBL:KOY88145.1, ECO:0000313|Proteomes:UP000037950};
RN [1] {ECO:0000313|EMBL:KOY88145.1, ECO:0000313|Proteomes:UP000037950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=336/3 {ECO:0000313|EMBL:KOY88145.1,
RC ECO:0000313|Proteomes:UP000037950};
RA Isojarvi J., Battchikova N., Aro E.-M.;
RT "Draft genome sequence of symbiotic bacteroides-like organism.";
RL Submitted (JUL-2015) 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:KOY88145.1}.
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DR EMBL; LJIE01000001; KOY88145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0CZX6; -.
DR STRING; 1664068.AD998_10310; -.
DR PATRIC; fig|1664068.3.peg.2097; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000037950; 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:UP000037950}.
FT DOMAIN 14..441
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 464..731
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 780..900
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 968 AA; 106846 MW; 0169AA58FB23C79B CRC64;
MKINLTQSEK FENRHHGYFG KDFQEMLATV GVKSLDELIE QTVPASIRLK SPLKVTEPQG
EHEFLQNFKK IAQKNKVFKS YIGMGYYDTF TPNVILRNIL ENPAWYTAYT PYQAEIAQGR
LEALINYQTM VIDLTGMEIA NASLLDEATA AAEAMNMLYA QKKAEKKDAH TIFVSQELFP
QTIDVLKTRA IPVGINIEVG DHNKVDLTRK DLYAVFVQYP AQNGDVYDYT DFIATAKEQN
VFVAVASDLL ALTILKSPGE MGADVVIGSS QRFGVPMGYG GPHAAFFATK EEYKRHIPGR
IIGVSIDAHG NKAYRMALQT REQHIRREKA TSNICTAQVL LSVMAGMYGV YHGAEGLQQI
AQKVYGLAEL LKKGLTSLGY TVQNQNHFDT LKIAVTDKTA IQKIAEAKEV NFRYFENENS
ISVALDETTT IADIKVVLQI LAEAKNTNLS FDVEQESQNI SLSLPENLVR KSSYMTHPVF
NTYHTEHEML RYMKQLENKD LSLVHSMISL GSCTMKLNAT AEMIPVTWAE MGKIHPFVPQ
YQALGYKEMI DSLSTWLAEI TGFDAVSMQP NSGAQGEYAG LMVIRAYHES RGEGHRNIAL
IPASAHGTNP ASAVMAGMHV VVTKTDENGN IDVADLKAKA EQYKDSLSCL MVTYPSTHGV
FEESIQEICA LIHSYGGQVY MDGANMNAQV GLTSPGNIGA DVCHLNLHKT FCIPHGGGGP
GMGPICMKAH LAPFMANHSV VKFLDNNMSA VSAAPFGSSS ILAISYTYIA MMGGAGLTRA
TQMAILNANY IKERLAGHYP VLYSGKNGRA AHEMILDCRP FKAFGVEAED IAKRLMDYGF
HAPTLSFPVA GTLMVEPTES ESKAELDRFC DAMIEIRNEI REIEQGKYDQ KVNVLKNAPH
TAQIALAENW TLPYTREKAV FPLAYVKKTK FWPAVSRIDS AYGDRNLICS CIPVEAYAQE
EKTAGATA
//
