ID A0A3L9MAJ2_9FLAO Unreviewed; 953 AA.
AC A0A3L9MAJ2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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:RLZ07549.1};
GN ORFNames=EAH69_11295 {ECO:0000313|EMBL:RLZ07549.1};
OS Flavobacteriaceae bacterium YIM 102668.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=2479857 {ECO:0000313|EMBL:RLZ07549.1, ECO:0000313|Proteomes:UP000275348};
RN [1] {ECO:0000313|EMBL:RLZ07549.1, ECO:0000313|Proteomes:UP000275348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 102668 {ECO:0000313|EMBL:RLZ07549.1,
RC ECO:0000313|Proteomes:UP000275348};
RA Chen X.;
RL Submitted (OCT-2018) 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:RLZ07549.1}.
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DR EMBL; RDOJ01000017; RLZ07549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L9MAJ2; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000275348; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:RLZ07549.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50}.
FT DOMAIN 9..436
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 470..722
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 772..892
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT COILED 617..644
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 700
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 953 AA; 104962 MW; 51DB888F12CFAF68 CRC64;
MNTNDFSIRH IGNNAKQAAE MLAVIGKDSI DSLVEATLPQ NIRLKKELEL PEALSEFEAT
NHLAELASLN QKVKNYLGYG YYGTILPAPI QRNVLENPGW YTAYTPYQAE IAQGRLEALL
NFQTVISDLT GLPIANASLL DEGTACGEAM HMLFESRSRD QKKNNVNKFF IADNLFPQSV
AVLETKAHGL GIEVVIGNFE TTEITEEFFG AIVQYIGKGG QINNYKSFVE KANAVGVKVA
VATDLLALTL LTPPGEWGAD ITIGTSQRFG VPMGYGGPHA AFMSCTEDYK RVIPGRIIGV
SQDRLGNYAL RMALQTREQH IKREKATSNI CTAQVLLAVM ASFYAVYHGK DGLKFIAEEI
HTKAAILHGG LQHLGYNLVN TNFFDTVQIA VENSDEIVKI FADEEINVNG FEKGKVSITV
DEMTSEEDIF EILSVFATIN NTEEGFEFEV DESFLPADLI RTTDFLTHPN FNSFHTETEL
MRYIKRLERK DLALNQSMIA LGSCTMKLNA ATQLLHMSWE RMGNVHPFTP KEQVEGYQTL
IKNLEDYLSE ITGFDATSLQ PNSGAQGEYA GLMVIRSYFE SKGEGHRNVA LIPQSAHGTN
PASAAMAGMK VVVVKNLESG ETDLEDLKAK CELHKDNLAA LMITYPSTYG AFDSNIEEVT
TMIHEYGGQV YMDGANMNAQ VGLTSPGNIG ADVCHLNLHK TFAIPHGGGG PGVGPICVKS
HLAPFLGSSP LIETGGKETT NTFAAAPYGS AFILPISYTY ILMLGAEGLL KSTQGAILNA
NYMKTRLEGH YDILYTNAQN VVAHEFILDC RPFKKVGVEV TDIAKRLIDY GFHAPTVSFP
VAGTLMVEPT ESETKAELDR FCDALIAIRQ EIDEVANGDF PVDNNVLHNA PHPQHLLTAD
EWEYPYTRSK AAFPLEWVRE RKFFATVSRI DDAYGDRNLM CTCAPIEDYI DQD
//
