ID K2Q4T5_9FLAO Unreviewed; 949 AA.
AC K2Q4T5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=I215_04720 {ECO:0000313|EMBL:EKF55826.1};
OS Galbibacter marinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Galbibacter.
OX NCBI_TaxID=555500 {ECO:0000313|EMBL:EKF55826.1, ECO:0000313|Proteomes:UP000007364};
RN [1] {ECO:0000313|EMBL:EKF55826.1, ECO:0000313|Proteomes:UP000007364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ck-I2-15 {ECO:0000313|Proteomes:UP000007364};
RX PubMed=23209227; DOI=10.1128/JB.01852-12;
RA Lai Q., Li C., Shao Z.;
RT "Genome Sequence of Galbibacter marinum Type Strain ck-I2-15.";
RL J. Bacteriol. 194:6973-6973(2012).
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:ARBA00043839, 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}.
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:EKF55826.1}.
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DR EMBL; AMSG01000004; EKF55826.1; -; Genomic_DNA.
DR RefSeq; WP_008990817.1; NZ_AMSG01000004.1.
DR AlphaFoldDB; K2Q4T5; -.
DR STRING; 555500.I215_04720; -.
DR PATRIC; fig|555500.3.peg.977; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000007364; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007364}.
FT DOMAIN 9..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 470..728
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|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 949 AA; 104232 MW; B286543838845700 CRC64;
MKTDSFVTRH VGPQEDDLNS MLNVIGVDTI DELIAQTVPA GIRLKDELDL PPAMSEYEYL
GHLKNLAKKN KVFRTFIGLG YHESITPSVI KRNILENPGW YTAYTPYQAE IAQGRLEALL
NFQTMVCDLT GMEIANASLL DEGTAAAEAM SMLFSVRSRD QKKNGANKFF VSDQVLPQTI
SILKSHAAPL DIELQIDTYE NFDFSSDYFG ALLQYPGKFG AVYNYHEFVA KANENEIKVA
VAADILSLVS LTPPGEFGAE VVVGTTQRFG IPLGYGGPHA AYFATKEAYK RNIPGRIIGV
TRDMDGRIGL RMALQTREQH IKRDKATSNI CTAQVLLAVM AGMYAVYHGP KGLKYIADKV
HHSAVSLSDA LKSLGYQQNN ASYFDTLLIE ADASKIRPLA EAQQINFLYP KEDKVAISLN
ETVSLNDLNA IVRIFAEAAG KTANDISEIT QKTTILEENQ RQSPFMENEV FNNYHSETEL
MRYIKKLERK DLALNHSMIS LGSCTMKLNA ASEMLPISWD EWGNIHPFVP LNQAEGYLEV
LNELEHQLNV ITGFAGTSLQ PNSGAQGEFS GLMVIRAYHE ANGQGHRNIC LIPASAHGTN
PASAALAGFK VVVTKTDEKG NIDVQDLGEK AEKYKDELAA LMVTYPSTHG VFESSIKEIT
EIIHRNGGQV YMDGANMNAQ VGLTNPATIG ADVCHLNLHK TFAIPHGGGG PGVGPICVAP
HLVEFLPSNP IITTGGDNAI EAISSAPFGS SLVCLISYGY IKMLGRKGLK TATHAAILNA
NYIKAKLTGT FEVLYTGEKG RAAHEMIIDC RPFKAKGIEV TDIAKRLIDY GFHAPTVSFP
VAGTIMIEPT ESESVDELDR FCEALISIKN EIDQITDINA ENILKNAPHT LRMVTSDTWE
FPYSRTEAAY PLPYVAENKF WPTVRRVDEA YGDRNLMCTC PPIEAYMEA
//
