ID A0A2A2T9Y2_9CYAN Unreviewed; 421 AA.
AC A0A2A2T9Y2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
DE Flags: Fragment;
GN ORFNames=CK510_29755 {ECO:0000313|EMBL:PAX45803.1};
OS Calothrix elsteri CCALA 953.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=987040 {ECO:0000313|EMBL:PAX45803.1, ECO:0000313|Proteomes:UP000218238};
RN [1] {ECO:0000313|EMBL:PAX45803.1, ECO:0000313|Proteomes:UP000218238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 953 {ECO:0000313|EMBL:PAX45803.1,
RC ECO:0000313|Proteomes:UP000218238};
RA Gagunashvili A.N., Elster J., Andresson O.S.;
RT "Draft genome sequence of filamentous cyanobacterium Calothrix elsteri
RT CCALA 953.";
RL Submitted (AUG-2017) 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}.
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};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:PAX45803.1}.
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; NTFS01000674; PAX45803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2T9Y2; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000218238; Unassembled WGS sequence.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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 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 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; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000218238}.
FT DOMAIN 94..200
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 241..362
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PAX45803.1"
SQ SEQUENCE 421 AA; 45368 MW; CB2C35386C348511 CRC64;
SQTKGYQILF EQLEEWLGEI TGFAGISLQP NAGSQGEYTG LLVIRQYHQS RGESDRNICL
IPESAHGTNP ASAVMCGMKV VPVACDNDGN VDITDLKGKA EKHSKQLSAL MVTYPSTHGV
FEEGIKEICA IVHSHGGQVY MDGANMNAQV GLCRPGDIGA DVCHLNLHKT FCIPHGGGGP
GMGPIGVAAH LVPFLPGHTV IEIGGEKAIG AVSAAPWGSA SILVISWMYI VMMGASGLTA
ATKIAILNAN YIAKRLEGYY PVLYKGSNGY VAHECILDLR ALKKSANIEI DDLAKRLMDY
GFHAPTVSWP VAGTIMVEPT ESESQEELDR FCDALIAIRG EIAAIESGKM DIQDNLLKNA
PHTAESLISG EWTHPYTREE AAYPAPWTRD SKFWVSVSRI DAAFGDRNFV CSCLPMDAYV
E
//
