ID A0A0D6TMJ8_9FLAO Unreviewed; 947 AA.
AC A0A0D6TMJ8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN ORFNames=SY27_07100 {ECO:0000313|EMBL:KIX21469.1};
OS Flavobacterium sp. 316.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1603293 {ECO:0000313|EMBL:KIX21469.1, ECO:0000313|Proteomes:UP000032747};
RN [1] {ECO:0000313|EMBL:KIX21469.1, ECO:0000313|Proteomes:UP000032747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=316 {ECO:0000313|EMBL:KIX21469.1,
RC ECO:0000313|Proteomes:UP000032747};
RA Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P.,
RA Madanecki P., Markert S., Piotrowski A., Schweder T., Szalewska-Palasz A.;
RT "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a
RT Genomic and a Proteomic Perspective.";
RL Submitted (FEB-2015) 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}.
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:KIX21469.1}.
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DR EMBL; JYGZ01000003; KIX21469.1; -; Genomic_DNA.
DR RefSeq; WP_045968643.1; NZ_JYGZ01000003.1.
DR AlphaFoldDB; A0A0D6TMJ8; -.
DR STRING; 1603293.SY27_07100; -.
DR PATRIC; fig|1603293.4.peg.1468; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000032747; 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 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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000032747}.
FT DOMAIN 9..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 471..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|PIRSR:PIRSR603437-50"
SQ SEQUENCE 947 AA; 103993 MW; 570511385B32A487 CRC64;
MRTDAFALRH IGPRENDLEK MFSTVGVENM EQLIYETIPD DIRLQSNLDL DAAMTEYEYL
NHIQELGKKN KVFTSYIGLG YHPTIVPAVI QRNIFENPGW YTAYTPYQAE IAQGRLEAIL
NFQTTVIELT GMEIANASLL DESTAAAEAM ALLFDVRTRD QKKNNVNKFF VSEEILPQTL
SLLQTRSTPI GVELVIGNHE TFDFSTDFFG AILQYPGKYG QVNDYTNFIA KANANDIKVG
VAADILSLVK LTPPGEMGAA VVVGTTQRFG IPMGYGGPHA AFFATKEEYK RSMPGRIIGV
SQDANGNRAL RMALQTREQH IKREKATSNI CTAQVLLAVM AGMYAVYHGP KGLKYIASKV
HASAVTAAEA LNKIGVYQTN TSFFDTIVVK ADAEKVRTIA EKNEVNFYYI DNETISISFN
ETTSLQDINK VIAIFAEAVG KETTKVTALT TENNFPTLLE RKSEFLQHEV FNNHHSESQL
MRYIKKLERK DLSLNHSMIS LGSCTMKLNA AAEMLPLSMA NWNSIHPFAP IEQAEGYQIV
LKKLEQQLNV ITGFQGTTLQ PNSGAQGEYA GLMAIRAYHI SNGNAHRNVC LIPASAHGTN
PASAAMAGMK IIVTKTTEKG NIDVEDLRAK AIEHAADLSC LMVTYPSTHG VFESTIKEVT
KIIHDNGGLV YMDGANMNAQ VGLTNPATIG ADVCHLNLHK TFAIPHGGGG PGVGPICVND
KLVPFLPSNP IIKVGGEQAI TAISAAPYGS ALVCLISYGY ISMLGSEGLT NATKHAILNA
NYMKARLEEH YPVLYSGEMG RAAHEMILDC RGFKVKGIEV TDIAKRLMDY GFHAPTVSFP
VAGTLMIEPT ESEDIAELDR FCDAMISIRK EIEAATAEEP NNELKNAPHT LAMLTANTWE
LPYSREKAAY PLEYVAENKF WPSVRRVDDT YGDRNLVCSC APIEAYI
//
