ID G2Z0R1_FLABF Unreviewed; 947 AA.
AC G2Z0R1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN Name=gcvP {ECO:0000313|EMBL:CCB69456.1};
GN OrderedLocusNames=FBFL15_1383 {ECO:0000313|EMBL:CCB69456.1};
OS Flavobacterium branchiophilum (strain FL-15).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1034807 {ECO:0000313|EMBL:CCB69456.1, ECO:0000313|Proteomes:UP000009186};
RN [1] {ECO:0000313|EMBL:CCB69456.1, ECO:0000313|Proteomes:UP000009186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FL-15 {ECO:0000313|EMBL:CCB69456.1,
RC ECO:0000313|Proteomes:UP000009186};
RX PubMed=21926215; DOI=10.1128/AEM.05625-11;
RG 1:IP;
RG Microbial Evolutionary Genomics,F-75015 Paris;
RG France 2:CNRS;
RG URA2171;
RG F-75015 Paris,France 3:Unite de Virologie et Immunologie Mol.;
RG INRA,78352 Jouy en Josas Cedex;
RG France. 4:Unite de Mathemathique;
RG Informatique et Genome,INRA;
RG 78352 Jouy en Josas Cedex;
RG France. 5:CEA/Genoscope;
RG Evry;
RG France;
RA Touchon M., Barbier P., Bernardet J.F., Loux V., Vacherie B., Barbe V.,
RA Rocha E.P., Duchaud E.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT branchiophilum.";
RL Appl. Environ. Microbiol. 77:7656-7662(2011).
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:ARBA00033655};
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; FQ859183; CCB69456.1; -; Genomic_DNA.
DR RefSeq; WP_014083923.1; NC_016001.1.
DR AlphaFoldDB; G2Z0R1; -.
DR STRING; 1034807.FBFL15_1383; -.
DR KEGG; fbr:FBFL15_1383; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_3_2_10; -.
DR OMA; CVPMSEY; -.
DR Proteomes; UP000009186; 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; 1.
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 ECO:0000313|EMBL:CCB69456.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000009186}.
FT DOMAIN 9..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 453..727
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 947 AA; 104487 MW; 43716E59FEEC2975 CRC64;
MKTDAFALRH IGPSENDVQK MLQFIGVSST EQLISETIPA DIRLKKPLEL APAMTEYEFA
NHIHELGNKN KIFKSYIGLG YNQAVVPAVI QRNIFENPGW YTAYTPYQAE IAQGRLEAIL
NFQTMVIELT GMEIANASLL DEGTAAAEAM ALLFDVRTRD QKKNNVNKFF VSEAIFPQTL
SVLQTRAMPI GIEIVIGNHE NFDFSSGYFG AILQYPAKFG QIYDYTDFIT KAKSNDIKVA
VAADILSLTI LTPPGEMGAD VVVGTTQRFG IPLGYGGPHA AYFATKDEYK RSMPGRIIGI
TIDADGNRAL RMALQTREQH IKRDKATSNI CTAQVLLSVM AGMYAVYHGP KGLQYIANTI
QSLAYNLAKE LHNLGYIQKN TSYFDTIVIE AEQSIIQPLA EAQSYNFYYI DEKNIAISLN
ETTSINDVNK ILEIFASAKG QSVEKLNSLD ENSAIPLHLN RKSAFLQHEV FNKYHSESAL
MRYIKMLERK DLSLNHSMIS LGSCTMKLNA ASEMLPLSNP QWNNMHPFAP INQALGYQEM
LSKLEQQLSI ITGFAGTTLQ PNSGAQGEYA GLMVIRAYHH ARGDFHRNIA LIPSSAHGTN
PASAAMAGMQ IIVTKTLENG NIDVEDVREK AILYKDNLSC LMVTYPSTHG VFESTIKEIS
QIIHENGGQV YMDGANMNAQ VGLTNPATIG ADVCHLNLHK TFAIPHGGGG PGVGPICVAP
QLVPFLPSNP IIQTGGSQAI TAISAAPWGS ALVCLISYGY ICMLGEEGLS KATTMAILNA
NYIKERLNGH YDTLYSGEQG RAAHEMILEC RPFKQKGIEV TDIAKRLMDF GFHAPTVSFP
VAGTLMIEPT ESENLDELDR FCEAMISIRQ EIENASIEDK NNVLKNAPHT QAMLTADEWN
FPYTRTQAAF PLDYLKENKF WPTVRRADDA FGDRNLVCSC VPIEAYQ
//