ID A0A0F6QWR5_9CORY Unreviewed; 944 AA.
AC A0A0F6QWR5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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:AKE39557.1};
GN ORFNames=UL81_08015 {ECO:0000313|EMBL:AKE39557.1};
OS Corynebacterium camporealensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=161896 {ECO:0000313|EMBL:AKE39557.1, ECO:0000313|Proteomes:UP000033566};
RN [1] {ECO:0000313|EMBL:AKE39557.1, ECO:0000313|Proteomes:UP000033566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44610 {ECO:0000313|EMBL:AKE39557.1,
RC ECO:0000313|Proteomes:UP000033566};
RX PubMed=26021938;
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete Genome Sequence of Corynebacterium camporealensis DSM 44610,
RT Isolated from the Milk of a Manchega Sheep with Subclinical Mastitis.";
RL Genome Announc. 3:e00572-15(2015).
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}.
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DR EMBL; CP011311; AKE39557.1; -; Genomic_DNA.
DR RefSeq; WP_035105276.1; NZ_CP011311.1.
DR AlphaFoldDB; A0A0F6QWR5; -.
DR KEGG; ccj:UL81_08015; -.
DR PATRIC; fig|161896.4.peg.1570; -.
DR HOGENOM; CLU_004620_2_1_11; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000033566; 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:AKE39557.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000033566}.
FT DOMAIN 6..426
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 454..707
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 762..882
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 684
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 944 AA; 101782 MW; 3A26C7647C34A57C CRC64;
MNFISRHLGP DATEREQMLA KLGYDSVEDL VDAAIPQKIR AEESLQLPEP LSEDDAQAKL
RSYAQHNQVL KSFYGQGFSD TLTPAVIRRG MLEDAGWYTA YTPYQPEISQ GRLEALLNFQ
TMIQSLTGLP IANASLLDEA SATAEAVGLM SRAVKKGRRV VLDSRLHPQV LTVAAERARA
IELEVEITDV RDGIVGEDLV GAVIAYTGTE GDIFDPRSVI EELQTRGAKA AVVADPLSLM
LLEAPGEMGA DIVLGSSQRF GVPLFFGGPH AAFMAVSEKL KRQMPGRIVG VSKDADGRPA
YRLALQTREQ HIRRERATSN ICTAQALLAN VASMYAVYHG PQGLEDIAKR VHTLASSFAQ
AVKDAGKELV SEEFFDTVTV AGVDAAAIKS ALQEAGYLVR TIGDDKVSVS FGESATQGDV
HVLADAFGAK AGDEADFAFP EGVQRSEQPL QHEIFNTIHS ETQMMRYLRK LADKDLALDR
TMIPLGSCTM KLNPTAAMEP ISWPEFANIH PYAPEETTAG WRELIDELEG WLAELTGYAK
VSIQPNAGSQ GELAGLLAIR RYHVANGDNG RDVVLIPASA HGTNAASATL ANLRVAVVKT
ADDGSIDLAD LDAKIEQYNE HIAGIMITYP STHGVFDPEV RDVCDKIHAA GGQVYIDGAN
MNALTGWARP GQFGGDVSHL NLHKTFTIPH GGGGPGVGPV GVAEHLIPFL PTNAADPELD
ATEATPVGQG VPITNTQYGS AGVLPISWAY LAMAGANGLA DASSHAILGA NYVAHELNDS
FPVLYTGNKG LVAHECILDL RELTDKSGVT AADVAKRLID FGFHAPTLAF PVAGTLMVEP
TESEDLGELD RFIEAMRTIR AEIQEIIDGD VAYEDSVVHH APFTAVSLIN EDWDYKFDRE
KAAYPVNSLR LNKYFPPVRR LDEAYGDRNL VCSCPPPEAF DIED
//
