ID A0A1D9P7X9_9FLAO Unreviewed; 949 AA.
AC A0A1D9P7X9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN ORFNames=BIW12_03755 {ECO:0000313|EMBL:AOZ98622.1};
OS Flavobacterium commune.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1306519 {ECO:0000313|EMBL:AOZ98622.1, ECO:0000313|Proteomes:UP000178198};
RN [1] {ECO:0000313|EMBL:AOZ98622.1, ECO:0000313|Proteomes:UP000178198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PK15 {ECO:0000313|EMBL:AOZ98622.1,
RC ECO:0000313|Proteomes:UP000178198};
RA Ekwe A., Kim S.B.;
RT "Complete Genome Sequence of Flavobacterium sp. PK15.";
RL Submitted (OCT-2016) 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 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}.
CC -!- SIMILARITY: Belongs to the GcvP family.
CC {ECO:0000256|ARBA:ARBA00010756}.
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DR EMBL; CP017774; AOZ98622.1; -; Genomic_DNA.
DR RefSeq; WP_071183874.1; NZ_CP017774.1.
DR AlphaFoldDB; A0A1D9P7X9; -.
DR STRING; 1306519.BIW12_03755; -.
DR KEGG; fcm:BIW12_03755; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000178198; Chromosome.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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 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};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000178198}.
FT DOMAIN 9..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 441..723
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 772..889
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 700
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 949 AA; 104169 MW; E179BDE54E69DDD2 CRC64;
MKTDAFALRH IGPEESDLQH MLKTIGVDSI EQLIYETLPD DIRLKAPLNL DPEMTEYEYL
KHITLLGSKN KMFKTYIGLG YNQAIVPAVI QRNVFENPGW YTAYTPYQAE IAQGRLEAIL
NFQTMVIELT GMEIANASLL DEGTAAAEAM ALLFDVRTRE QKKANVCKFF VSEEILPQTL
SVLQTRSTPI GVELVIGNHE NFDFSDEFFG AILQYPGKFG QVNDYTPFIA KAAENNIKVA
VAADILSLAK LTPPGEMGAA VVLGTTQRFG IPLGYGGPHA AYFATKEEYK RSMPGRIIGV
TVDTNGNRAL RMALQTREQH IKRDKATSNI CTAQVLLSVM ASMYAVYHGP RGLRYIANKV
HASAVTLANT LAKLGFEQTN TAFFDTIVIK ADAKKIREIA EANEVNFFYP NENSVSISLN
ETIGFADLNK VVSIFAAAKE LATITISELS ETNHFPESLI RTSTFLQHEV FNKYHSETAL
MRYIKMLERK DLALNHSMIS LGSCTMKLNA AAEMLPLSSP SWNSIHPFAP LDQAKGYQKM
LSKLEEYLNE ITGFAATTLQ PNSGAQGEYA GLMVIQAYHE SRGDHHRNIA LIPASAHGTN
PASAAMAGMK VVVTKTLENG NIDVEDLREK AILHKDNLSC VMITYPSTHG VYESAIKEIT
KIVHDNGGQV YMDGANMNAQ VGLTNPATIG ADVCHLNLHK TFAIPHGGGG PGVGPICVAP
QLAPFLPTNP VVPTGGENAI TAISAAPWGS ALVCLISYGY IKMLGAEGLK SATEHAILNA
NYIKEKLSGH YDTLYSGEMG RAAHEMILEC RPFKQKGIEV TDIAKRLMDY GFHAPTVSFP
VAGTLMIEPT ESENLEELDR FCDAMISIRK EIEAASIEDS NNVLKNSPHT LAMLTTENWD
FPYSREQAAF PLDYIAENKF WPSVRRADDA FGDRNLVCSC APIEAYMES
//
