ID X5DXM3_9CORY Unreviewed; 971 AA.
AC X5DXM3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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:AHW65317.1};
GN ORFNames=CGLY_14405 {ECO:0000313|EMBL:AHW65317.1};
OS Corynebacterium glyciniphilum AJ 3170.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1404245 {ECO:0000313|EMBL:AHW65317.1, ECO:0000313|Proteomes:UP000023703};
RN [1] {ECO:0000313|EMBL:AHW65317.1, ECO:0000313|Proteomes:UP000023703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AJ 3170 {ECO:0000313|EMBL:AHW65317.1};
RX PubMed=25323597; DOI=10.1099/ijs.0.065102-0;
RA Al-Dilaimi A., Bednarz H., Lomker A., Niehaus K., Kalinowski J.,
RA Ruckert C.;
RT "Revisiting Corynebacterium glyciniphilum (ex Kubota et al., 1972) sp.
RT nov., nom. rev., isolated from putrefied banana.";
RL Int. J. Syst. Evol. Microbiol. 65:177-182(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; CP006842; AHW65317.1; -; Genomic_DNA.
DR RefSeq; WP_038550327.1; NZ_CP006842.1.
DR AlphaFoldDB; X5DXM3; -.
DR STRING; 1404245.CGLY_14405; -.
DR KEGG; cgy:CGLY_14405; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_2_1_11; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000023703; 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:AHW65317.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000023703}.
FT DOMAIN 10..439
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 479..725
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 778..899
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 703
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 971 AA; 103167 MW; C34B7EDDC8902AEB CRC64;
MATPHDAFPN RHIGPDADAT SDILTTLGYG SSQELAAAAL PASIAQQGPI GLAPALDETE
ALATLRGFAA KNTVKKQLIG AGYYDTVTPA VIRRNVVENP GWYTAYTPYQ PEISQGRLEA
LLNFQTMVED LTGLPIAGAS LLDEATAVAE AVQMMARLNT KAAKKGGVVL LDAALHASSI
NITRARAAAV DIPVEIVDIT AETVAAREDA LIGVVVSNPG TTGGLRDDLG EVIAAVHEQD
GLVTVACDLL AQVLVTSPGE LGADIAVGSA QRFGVPLFFG GPHAAFLACR ENMQRKLPGR
IVGVSVDAEG TPAYRLSLQT REQHIRRDKA TSNICTAQAL LAVVASFYAV WHGPQGLREI
ATAVHGRATA LAVGLSEAGL TLAHDRFFDT VTVQVQDAAA TVAAACDKGF NLRHVDDTHV
GVSVGESTTD GDIAELLQVI GNVASSVTTT EFTAQDGPLS DLLRTDDILT HPVFHSVSSE
TQMMRYMRRL ADRDLALDRT MIPLGSCTMK LNAAVSMEPI TWPEFAGIHP MVPEDQATGW
WELIDDLEGR LAKITGYAAV SVQPNAGSQG ELAGLLAIRR FHVANGDDQR TLVLIPASAH
GTNAASAALA GLKVVGVKNA EDGSVDLDDL DAKIEKYGEQ IAGIMITYPS THGVFEEHVR
EVCSKVHATG GQVYIDGANL NALVGLAQPG EFGGDVSHLN LHKTFTIPHG GGGPGVGPVC
VGEHLIPFLP SDPWADVTVE PDAQEGRPVS AANQGSAGVL PISWTYIAMM GDEGLTEASR
MALVNANYIS RQLADSFPTL YTGENGLVAH ECILDLRDLT KQSGVTAADV TKRLMDFGFH
APTLAFPVAG TLMVEPTESE DKHELDRFIT ALRTIRAEID EVIAGDVAVE DSVLRHAPFT
AESVIRDDFE DAVSHGHFSR EKAAFPVRTL RRDKYFPAVR RIDDAYGDRN LMCSCPPLEN
FDIEADIESE N
//
