ID D5BZ60_NITHN Unreviewed; 452 AA.
AC D5BZ60;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
GN Name=gcvPA {ECO:0000256|HAMAP-Rule:MF_00712};
GN OrderedLocusNames=Nhal_1101 {ECO:0000313|EMBL:ADE14273.1};
OS Nitrosococcus halophilus (strain Nc4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE14273.1, ECO:0000313|Proteomes:UP000001844};
RN [1] {ECO:0000313|Proteomes:UP000001844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844};
RG US DOE Joint Genome Institute;
RA Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., Ward B.B.,
RA Klotz M.G.;
RT "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt-adapted,
RT aerobic obligate ammonia-oxidizing sulfur purple bacterium.";
RL Submitted (APR-2010) 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_00712}.
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_00712};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. In this organism, the P 'protein' is a heterodimer of two
CC subunits. {ECO:0000256|HAMAP-Rule:MF_00712}.
CC -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00712}.
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DR EMBL; CP001798; ADE14273.1; -; Genomic_DNA.
DR RefSeq; WP_013032165.1; NC_013960.1.
DR AlphaFoldDB; D5BZ60; -.
DR STRING; 472759.Nhal_1101; -.
DR KEGG; nhl:Nhal_1101; -.
DR eggNOG; COG0403; Bacteria.
DR HOGENOM; CLU_004620_0_2_6; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000001844; Chromosome.
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 GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR CDD; cd00613; GDC-P; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00712; GcvPA; 1.
DR InterPro; IPR023010; GcvPA.
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 PANTHER; PTHR42806; GLYCINE CLEAVAGE SYSTEM P-PROTEIN; 1.
DR PANTHER; PTHR42806:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR Pfam; PF02347; GDC-P; 1.
DR PIRSF; PIRSF006815; GcvPA; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00712}; Reference proteome {ECO:0000313|Proteomes:UP000001844}.
FT DOMAIN 3..440
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
SQ SEQUENCE 452 AA; 48656 MW; 736B715DC7E1B3D3 CRC64;
MPFIPHTDED IRSMLATIGV PDIEALFDEI PAALRTTDFD AVPPGLNEIE VTRLLRGRAA
QNHAAICFAG GGAYQHHIPA PIWEITSRGE YYSAYTPYQA EASQGTLQVI YEYQSMVAAL
TGMEVSNASI YDGASALGEA VLMAVRLSRR GKSPRVLVPA TVHPAYRKVV ATLVQNQGIS
LEEIPYDIAS GAIDLEALES IKEDFAALVI PQPNYFGCLE EVDALTNWAH KQGGLVIGVV
NPTSLALLKP PGEWGEVGAD IVCGEGQPLG IPLASGGPYF GFMACKQAHV RQMPGRIVGR
TVDLENKPGY TLTLQAREQH IRRSKATSNI CTNQGLMVTA ATLYMGLLGP QGLAQVAAAC
HANTMALVKR LTAIPGVEQV FEKPFFHEAV LRFPVQASTV LSTLGQHGIL AGVRLDRTYP
ELGDTLLVCA TELRTEEEIE LYTRELAAAL PA
//
