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Database: UniProt
Entry: A0A346NSN5_9ALTE
LinkDB: A0A346NSN5_9ALTE
Original site: A0A346NSN5_9ALTE 
ID   A0A346NSN5_9ALTE        Unreviewed;       965 AA.
AC   A0A346NSN5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=D0Y50_14465 {ECO:0000313|EMBL:AXR08542.1};
OS   Salinimonas sediminis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Salinimonas.
OX   NCBI_TaxID=2303538 {ECO:0000313|EMBL:AXR08542.1, ECO:0000313|Proteomes:UP000262073};
RN   [1] {ECO:0000313|EMBL:AXR08542.1, ECO:0000313|Proteomes:UP000262073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N102 {ECO:0000313|EMBL:AXR08542.1,
RC   ECO:0000313|Proteomes:UP000262073};
RA   Cao J.;
RT   "Salinimonas sediminis sp. nov., a piezophilic bacterium isolated from a
RT   deep-sea sediment sample from the New Britain Trench.";
RL   Submitted (AUG-2018) 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:ARBA00033655, 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}.
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DR   EMBL; CP031769; AXR08542.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A346NSN5; -.
DR   KEGG; salm:D0Y50_14465; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000262073; 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   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}.
FT   DOMAIN          19..442
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          463..739
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          784..905
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   MOD_RES         711
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT                   ECO:0000256|PIRSR:PIRSR603437-50"
SQ   SEQUENCE   965 AA;  104818 MW;  9302CB97AD42CE2B CRC64;
     MTDTSKTLAQ LEQNNAFVRR HIGPGETEIS SMLQTINAES LDDLTQQTVP AGILLDKPIE
     TGEGASEVDA LSALKAVAAK NKINRSFIGM GYYDTHVPNV ILRNVLENPG WYTAYTPYQP
     EIAQGRLEAI LNFQQVTIDL TGLELASASL LDEGTAAAEA MALAKRVSKN KKANLFFIAD
     DVHPQTRDVV ETRAEMFGFG IVSGPTEQAS DHDVFGALLQ YPSTTGEVKD ISDTIAAVQA
     NKGIVAVAAD LMSLVMLKSP GELGADVALG SAQRFGVPMG YGGPHAAFFA TRDSYKRSLP
     GRIIGISKDT RGRPALRMAL QTREQHIRRE KANSNICTAQ VLLANMASFY AVYHGPEGLK
     TIASRIHRLA DILASGLKQK GLGLKHATWF DTLTVLTDNK ADVLQRAYAK GINLRADIDG
     AVGIALDETS TRNDVQALFD VLLGEGHNLQ VANLDDDVTT QGSQSIPASL RRTSDILQHE
     VFNQYHSETE MLRYIKSLEN KDLALNHSMI SLGSCTMKLN ATAEMIPVTW PEFGQLHPFA
     PLDQAAGYHE MISELAQWLI SITGYDAMSM QPNSGAQGEY AGLLAIQRYH ESRGEGHRNV
     CLIPSSAHGT NPASAQMVSL KVVVVNCDKN GNVDLKDLRA KAEEVGDNLS CAMITYPSTH
     GVYEETVREM CEIVHQYGGQ VYMDGANMNA QVGITAPGFI GSDVSHLNLH KTFCIPHGGG
     GPGMGPIGVK SHLAPFLPNH SVVDIDGAGK DCGAVSAAPW GSASILPISY MYIKMMGAEG
     LRKATQVAIL NANYVAKQLE GHFDVLYKGR NGRVAHECII DLRPLKEVSG VSEIDIAKRL
     NDYGFHAPTM SFPVAGTLMI EPTESEAKYE LDRFIEAMIS IRKEIAKVES GEWAADNNPL
     HFAPHTLADI CDSNWDRSYD RNLAAYPVAA VARNKFWPSV NRIDDVYGDR NLMCSCAPIE
     AYREE
//
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