GenomeNet

Database: UniProt
Entry: K9EXC6_9LACT
LinkDB: K9EXC6_9LACT
Original site: K9EXC6_9LACT 
ID   K9EXC6_9LACT            Unreviewed;       449 AA.
AC   K9EXC6;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
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   ORFNames=HMPREF9698_00645 {ECO:0000313|EMBL:EKU93850.1};
OS   Alloiococcus otitis ATCC 51267.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Alloiococcus.
OX   NCBI_TaxID=883081 {ECO:0000313|EMBL:EKU93850.1, ECO:0000313|Proteomes:UP000009875};
RN   [1] {ECO:0000313|EMBL:EKU93850.1, ECO:0000313|Proteomes:UP000009875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51267 {ECO:0000313|EMBL:EKU93850.1,
RC   ECO:0000313|Proteomes:UP000009875};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Alloiococcus otitis ATCC 51267.";
RL   Submitted (SEP-2012) 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}.
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:EKU93850.1}.
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; AGXA01000014; EKU93850.1; -; Genomic_DNA.
DR   RefSeq; WP_003777336.1; NZ_JH992958.1.
DR   AlphaFoldDB; K9EXC6; -.
DR   STRING; 883081.HMPREF9698_00645; -.
DR   PATRIC; fig|883081.3.peg.644; -.
DR   eggNOG; COG0403; Bacteria.
DR   HOGENOM; CLU_004620_0_2_9; -.
DR   OrthoDB; 9771867at2; -.
DR   Proteomes; UP000009875; 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   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:UP000009875}.
FT   DOMAIN          5..444
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
SQ   SEQUENCE   449 AA;  49924 MW;  661BB727382EA25E CRC64;
     MVHFRYLPNT DKDREEMLDV IGAKDIMDLY RDVPEEVQRK EPMNLPKPLS EYELLKEANR
     LASKNTTSNQ VPFFLGAGVY DHHVPTVVKH VIMRQEFLTA YVPYQPEVSQ GELQALFEWQ
     TMVAELTGMD LANSGLYDGY TAIGEANNLA IGQVRKSDKV LISKAVNPQG IQTAKTYGFG
     KNYDVEEVEL NGDITDLDDL KAKLDKNVAA VVVQYPNFFG SVEDLKAIKE LLEDYKTLLV
     VSSNPLALAK LEAPGHLGAD IVVGNIQPFG IPMQLGGPHS GYFAVTKKLM RKVPSRLVGE
     SVDEEGKRGF SMALSTREQH IRREKATSNY SSNQALFALA SAVALAAYGK QGVQELAQRN
     INNGHYLAKQ LQDKGFELLN SRPFFNEFTI KLDKDVEEVN KALYDKGYVG GYDASDALEQ
     EGAYLLVATE KRTKEEIDDF VQALAEVAK
//
DBGET integrated database retrieval system