ID A0A170WWM2_9ACTN Unreviewed; 961 AA.
AC A0A170WWM2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=STXM2123_2069 {ECO:0000313|EMBL:GAT81368.1};
OS Streptomyces sp. F-3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1840095 {ECO:0000313|EMBL:GAT81368.1, ECO:0000313|Proteomes:UP000078145};
RN [1] {ECO:0000313|EMBL:GAT81368.1, ECO:0000313|Proteomes:UP000078145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang L.S., Gao P.J., Liu L., Zhang H.Q., Cheng Z., Sun X.M.;
RT "Streptomyces sp. F-3 geneom sequencing.";
RL Submitted (MAY-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, 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:GAT81368.1}.
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DR EMBL; BDDR01000010; GAT81368.1; -; Genomic_DNA.
DR RefSeq; WP_067392574.1; NZ_BDDR01000010.1.
DR AlphaFoldDB; A0A170WWM2; -.
DR STRING; 1840095.STXM2123_2069; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000078145; 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:UP000078145}.
FT DOMAIN 19..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; 102921 MW; 0C1B5B6EF8B21C48 CRC64;
MTAQRIPLSE LEQGIPFEQR HIGADQEARA KMLAQVGYGS LDELMAAAVP DAIKSTDALD
LPGARTEAEV LAELRALAGR NQVLDSMIGL GYYGTFTPPV ILRNVLENPA WYTAYTPYQP
EISQGRLEAL LNFQTMVADL TGLPTAGASL LDEGTAAAEA MALSRRMGRN KKGLFLVDAD
ALPQTIAVLR TRAEPTGVEV VVADLSEGIP ADIAAREING VLLQYPGASG AVRDLKPVID
QAHELGALVT VAADLLALTL LKSPGELGAD IAVGTTQRFG VPMGFGGPHA GYMAVREKFA
RSLPGRLVGV SVDADGNQAY RLALQTREQH IRREKATSNI CTAQVLLAVM AGMYAVYHGP
EGLKGIARRT HRYATILAEG LRAGGAELVH DTYFDTLTVK AEGRAAEVVA AAREGGVNLR
LVDADHVSIA CDETTRRKHL HTVWAAFGVE GDVEALDAEA GDALPEALLR TDAYLTHPVF
HRYRSETAML RYLRRLADRD YALDRGMIPL GSCTMKLNAT TEMEPITWPE FGGLHPFAPV
EQAQGYLTLI RELEERLAEV TGYDKVSLQP NAGSQGELAG LLAVRAYHRA NGDDQRTVCL
IPSSAHGTNA ASAAMAGMKV VVVKTAENGE IDVEDLRAKI EQYRDQLAVL MITYPSTHGV
FEEHVADICA QVHEAGGQVY VDGANLNALV GLAKPGHFGG DVSHLNLHKT FCIPHGGGGP
GVGPVAVRAH LAPYLPNHPL QPEAGPGTGV GPVSAAPWGS AGILPISWAY LRLMGGEGLK
RATQMAVLSA NYIAKRLEPH YPVLYTGPGG LVAHECIIDL RPLTKATGVT VDDVAKRLID
YGFHAPTMSF PVAGTLMIEP TESEDLAELD RFCEAMIAIR AEIEKVASGA WPADDNPLRN
APHTASAISG PWEHPYSREE AVFPVGVPAA DKYWPPVRRI DQAYGDRNLV CSCPPLEAYE
D
//
