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Database: UniProt
Entry: G2Z0R1_FLABF
LinkDB: G2Z0R1_FLABF
Original site: G2Z0R1_FLABF 
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
//
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