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
//