ID A0A0N0SM58_9ACTN Unreviewed; 961 AA.
AC A0A0N0SM58;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000256|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000256|HAMAP-Rule:MF_00711};
GN ORFNames=ADK57_10460 {ECO:0000313|EMBL:KOU72014.1};
OS Streptomyces sp. MMG1533.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415546 {ECO:0000313|EMBL:KOU72014.1, ECO:0000313|Proteomes:UP000037741};
RN [1] {ECO:0000313|Proteomes:UP000037741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1533 {ECO:0000313|Proteomes:UP000037741};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00711, 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, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|HAMAP-Rule:MF_00711}.
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:KOU72014.1}.
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DR EMBL; LGDG01000066; KOU72014.1; -; Genomic_DNA.
DR RefSeq; WP_053749121.1; NZ_LGDG01000066.1.
DR AlphaFoldDB; A0A0N0SM58; -.
DR STRING; 1415546.ADK57_10460; -.
DR PATRIC; fig|1415546.3.peg.2280; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000037741; Unassembled WGS sequence.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00711; GcvP; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00711};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00711,
KW ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000037741}.
FT DOMAIN 20..447
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 454..736
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 782..903
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT COILED 626..653
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 709
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 961 AA; 102670 MW; CDAC619B7C1DFC84 CRC64;
MTAHRIPLSE LEQGIPFESR HIGPDQEARA KMLAQVGYGS LDELTAAAVP DVIKNADALE
LPGARTEAEV LAELRSLADR NQVLDSMIGL GYYGTFTPPV ILRNVMENPA WYTAYTPYQP
EISQGRLEAL LNFQTMVADL TGLPTSGASL LDESTAAAEA LALSRRMGKN KKGLFLVDAD
TLPQTIAVIE TRAEPTGVEV VVADLSDGIP AEIAGREING VLIQYPGASG AVRDIKPLIE
QAHELGALVT VAADLLALTL LKSPGELGAD IAVGTTQRFG VPMGFGGPHA GYMAVREKFA
RSLPGRIVGV SVDADGNKAY RLALQTREQH IRREKATSNI CTAQVLLAVM AGMYAVYHGP
EGLKSIARRT HRYATILAAG LTAGGVEVVH GSYFDTLTVH VPGRAAEIVA AARANGVNLR
LVDADHVSLA CDETTLRAQL GAVWSAFGVE GDIEALDAAT EETLPGALLR SDEYLAHPVF
HQYRSETAML RYLRRLADRD YALDRGMIPL GSCTMKLNAT TEMEPVTWPE FGQLHPFAPA
EQAQGYLTLI RELEERLAEV TGYDNVSLQP NAGSQGELAG LLAVRGYHRA NGDEQRTVCL
IPSSAHGTNA ASAVMAGMKV VVVKTAEDGE IDVEDLRAKI EQHRDELAVL MITYPSTHGV
FEEHVADICA QVHEAGGQVY VDGANLNALV GLAKPGHFGG DVSHLNLHKT FCIPHGGGGP
GVGPVGVRAH LAPYLPNHPL QPAAGPETGV GPISAAPWGA AGILPISWAY VRLMGGEGLK
RATQVAVLSA NYIAKRLEPH YPVLYTGPGG LVAHECIIDL RPLTKATGVS VDDVAKRLID
YGFHAPTMSF PVAGTLMIEP TESEDLTELD RFCEAMIAIR AEIEKVGSGE WPADDNPLRN
APHTAGALGG EWEHAYPREE AVFPAGVSVA DKYWPPVRRI DQAFGDRNLV CSCPPLDAYE
D
//
