ID A0A219AG80_9FLAO Unreviewed; 952 AA.
AC A0A219AG80;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:OWR13985.1};
GN ORFNames=CDW55_06495 {ECO:0000313|EMBL:OWR13985.1};
OS Chryseobacterium sp. VAUSW3.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=2010998 {ECO:0000313|EMBL:OWR13985.1, ECO:0000313|Proteomes:UP000243619};
RN [1] {ECO:0000313|EMBL:OWR13985.1, ECO:0000313|Proteomes:UP000243619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VAUSW3 {ECO:0000313|EMBL:OWR13985.1,
RC ECO:0000313|Proteomes:UP000243619};
RA Mayilraj S., Vyas B.;
RT "Chryseobacterium aquicola sp. nov isolated from upstream of the river
RT Ganges, Varanasi, India.";
RL Submitted (JUN-2017) 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:OWR13985.1}.
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DR EMBL; NIUY01000002; OWR13985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A219AG80; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000243619; 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; 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 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}.
FT DOMAIN 8..438
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 469..729
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 774..894
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 702
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 952 AA; 105524 MW; 9BB204D831132832 CRC64;
MNTTQFVNRH ISLNEADKQA MLQEIGVSGI DELIAQTIPD SIRLKEELNI SPALSEYEML
AHSKELAAKN SLFDNYIGFG YHNTILPSAI QRNILENPSW YTAYTPYQAE IAQGRLEALL
NFQTVVCDLT GFKLANASLL DESTAAAEAM HMFFESRTKD QRKSEAKKFF VSELVLPQTV
AVLKTKAEGL GIEIVEGDHE NHNFDESYFG VLLQYPGKNG IVLDYTENIK KYKEINLQVV
VASDPMALVK LKSPAEMGAD CAVGTTQRFG IPMGYGGPHA AFFACKEDYK RDIPGRIIGV
SQDAYGKRAL RMALQTREQH IKREKATSNI CTAQVLLAVM AGMYAVYHGP KGLNFIADQI
HFKANALNAG LKALGYDIVE EPVFDTVKFR MSEEEKKSLM FLMLDRKINL NYFTAGFVSI
ALNETTTLEK LQSLFDAFAQ FKDKQSFKLT LKEEILIPEQ SLRNDEILKE DVFNKYHTET
ELMRYIKRLE RKDLSLTHSM ISLGSCTMKL NAATQMLPIS WPEWGNVHPF VPTEQAGGYQ
QLIKELEKDL AEITGFAGTS LQPNSGAQGE YAGLMVIREY HKSRGESHRN IVLIPQSAHG
TNPASAVIAG MKVVVVKNLE SGEIDFEDLR AKAEQHAENL SAAMITYPST YGFFDDNIKE
ITKLIHDNGG QVYMDGANMN AQVGFTSPGN IGADVCHLNL HKTFAIPHGG GGPGVGPICV
AEHLVKFLPS NPNIKIGDKE AIDAISAAPY GSSLVLNISY AYIKMLGTAG LKKSTEHAIL
NANYLKEVLA EHFPILYANA AGRVAHECIV DFRQFKPLGI EVADVAKRLM DYGFHAPTVS
FPVAGTLMIE PTESESKTEI DRFAEALISI KKEIEEIAEG TADAANNVLK NAPHTEQVVI
SDAWDKPYSR EKAAYPLEWV RDHKFFATVS RVDEAYGDRN LICTCAPIES YM
//
