ID U7LF09_9CORY Unreviewed; 947 AA.
AC U7LF09;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN ORFNames=HMPREF1281_00303 {ECO:0000313|EMBL:ERS56521.1};
OS Corynebacterium sp. KPL1855.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1203562 {ECO:0000313|EMBL:ERS56521.1, ECO:0000313|Proteomes:UP000017096};
RN [1] {ECO:0000313|EMBL:ERS56521.1, ECO:0000313|Proteomes:UP000017096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KPL1855 {ECO:0000313|EMBL:ERS56521.1,
RC ECO:0000313|Proteomes:UP000017096};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Jacobson B., Goguen K.,
RA Pagano E., Lemon K.P., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Corynebacterium sp. KPL1855.";
RL Submitted (OCT-2013) 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:ERS56521.1}.
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DR EMBL; AXLX01000006; ERS56521.1; -; Genomic_DNA.
DR RefSeq; WP_023023151.1; NZ_KI515741.1.
DR AlphaFoldDB; U7LF09; -.
DR PATRIC; fig|1203562.3.peg.285; -.
DR HOGENOM; CLU_004620_2_0_11; -.
DR Proteomes; UP000017096; 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}.
FT DOMAIN 6..427
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 438..707
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 761..882
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 683
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 947 AA; 101550 MW; 20FD9A8F9FEA306A CRC64;
MDFISRHLGP DSSEQAAMLG TVGYDSVQAL VDAAIPPKIR ATELPHLPEA LSEDGAQAAL
REFANQNTVL KPFYGQGYSD TLTPAVIRRG LLEDAGWYTA YTPYQPEISQ GRLEALLNFQ
TMIESLTGLP IANASLLDEA SATAEAVGLM SRAVKKGRRV VLDSRLHPQV LTVAAERARA
IDLEVEIVDL REGLVGEDLI GAVIAYTGTE GEIFDPSAVI EELHTRGALA SVVTDPLSLL
LLEGPGNLGA DIVLGSSQRF GVPLFFGGPH AAYMAVTDKL KRQMPGRIVG VSKDADGRPA
YRLALQTREQ HIRRERATSN ICTAQALLAN VASMYAVYHG PKGLKDIAER VHSLSSSFAQ
SIVDAGLEIT SQHFFDTVTV CGVDAQKIKA DLQDAGYLVR AIGTDKVSVS FGESATQRDV
AHLAEAFGAT PAEANFDLPE NLQRAEEPLE HEIFHSIHSE TQMLRYLRKL ADKDLALDRS
MIPLGSCTMK LNPTAAMEPI SWPEFAGIHP YAPEETTAGW RALVEEIEGW LAELTGYAKV
SIQPNAGSQG ELAGLLAIRR YHVANGDNER DVVLIPASAH GTNAASATLA NLRVAVVKTA
EDGSIDVADL EEKIEKHGNH IAGIMVTYPS THGVFDPEVR DVCDKVHAVG GQVYIDGANM
NALTGWARPG DFGGDVSHLN LHKTFTIPHG GGGPGVGPVA VAEHLIPFLP SDAASPELDA
TAETPVGQGV PITGSKYGSA GVLPISWAYL AMTGAEGLAA ASGHAVLGAN YLAASLNEYF
PVLYTGNEGL VAHECIIDLR ELTDASGVTA ADVAKRLIDF GFHAPTLAFP VAGTLMIEPT
ESEDKGELDR FIEAMRTIRA EIQEIIDGEV AYEDSVIHHA PFTAESVATD NWEYSFGRDK
AAWPVKSLLH SYKYFPPVRR LDEAYGDRNL VCSCPPPEAF EIDDSEE
//
