ID A0A1F1USY9_9CORY Unreviewed; 950 AA.
AC A0A1F1USY9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN ORFNames=HMPREF3171_07760 {ECO:0000313|EMBL:OFT29230.1};
OS Corynebacterium sp. HMSC08F01.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1581139 {ECO:0000313|EMBL:OFT29230.1, ECO:0000313|Proteomes:UP000176366};
RN [1] {ECO:0000313|EMBL:OFT29230.1, ECO:0000313|Proteomes:UP000176366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC08F01 {ECO:0000313|EMBL:OFT29230.1,
RC ECO:0000313|Proteomes:UP000176366};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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:OFT29230.1}.
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DR EMBL; LWNT01000067; OFT29230.1; -; Genomic_DNA.
DR RefSeq; WP_070484032.1; NZ_KV789314.1.
DR AlphaFoldDB; A0A1F1USY9; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000176366; 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..425
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 436..706
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 950 AA; 102287 MW; AFF4491625386005 CRC64;
MDYISRHIGP NQDEQQQLLD ALGYESIDAL IAAAVPGGIL AEQPLDLPDA LTEYEAQARL
RELAGKNKVL RAFYGQGFNS TLTPPVIRRG VVEDAGWYTA YTPYQPEISQ GRLEALLNFQ
TMVQDLTGLD IANASLLDEA SAAAEAVGLM ARVVKKGRRV LLDARLHPQV INVAAERARA
IDLEVEVVDL TEGVVGEDLV GAVFAYPGTE GDVADPRPVI EAIHERGGLV AVDADILALT
LLESPGEFGA DIAIGTTQRL GVPLFYGGPH AAYMAVREKL QRQMPGRLVG VSKDAEGYPA
YRLALQTREQ HIRRERATSN ICTAQALLAV TASMYAVYHG PDGLTQIART IHQRATDFAV
ALEKAGVKVK HAEFFDTVAV EVDGARGVVD KFAQAGYLVR AIDDNTVGVS FGEDTTDADV
SALLAGFGAE AATGESRIPA ALVRKTEFLT HETFNRIHSE TQMMRYIREL GDKDLALDRT
MIPLGSCTMK LNPTAGLEAI TWPDFANVHP YTPDEYTEGW RELIDEIRSW LVEITGYAEV
SVQPNSGANG ELAGLLAIRR YHVANGDTER DICLIPASAH GTNAASATLA NLRVVVVKTA
ADGSIDINDL DEKLAKHEGH VAAIMLTYPS THGVYEEDVR VVCDKVHAAG GQVYIDGANM
NALTGIARPG DFGGDVSHLN LHKTFTIPHG GGGPGVGPIG VAEHLIPFLP SNPNVPLEQA
AAEIDGSAGV PVASTLFGSA GVLPISWSYI AMSGAAGLRS ATAHAVLNAN YIAKELNDSF
PVLYTGNNGL VGHECILDLR ELTDQSGVTA ADVAKRLVDY GFHAPTLAFP VAGTLMVEPT
ESEDLAEIDR FIEAMRSIRA EIQEIIDGKI EYENSVVHNA PYTAHSVARD EWPYEFTREQ
AAYPVDRLVH QKYFPPVRRV DEAFGDRNLQ CACPPPEAFD ITDDTNGTDN
//
