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Database: UniProt
Entry: V6JPL6_STRRC
LinkDB: V6JPL6_STRRC
Original site: V6JPL6_STRRC 
ID   V6JPL6_STRRC            Unreviewed;       961 AA.
AC   V6JPL6;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
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=M878_37915 {ECO:0000313|EMBL:EST21066.1};
OS   Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST21066.1, ECO:0000313|Proteomes:UP000017984};
RN   [1] {ECO:0000313|EMBL:EST21066.1, ECO:0000313|Proteomes:UP000017984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS 12.976 {ECO:0000313|EMBL:EST21066.1,
RC   ECO:0000313|Proteomes:UP000017984};
RX   PubMed=24407645;
RA   Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT   "Draft Genome Sequence of Streptomyces roseochromogenes subsp. oscitans DS
RT   12.976, Producer of the Aminocoumarin Antibiotic Clorobiocin.";
RL   Genome Announc. 2:e01147-e01113(2014).
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:EST21066.1}.
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DR   EMBL; AWQX01000334; EST21066.1; -; Genomic_DNA.
DR   RefSeq; WP_023552225.1; NZ_CM002285.1.
DR   AlphaFoldDB; V6JPL6; -.
DR   STRING; 1352936.M878_37915; -.
DR   PATRIC; fig|1352936.5.peg.7858; -.
DR   HOGENOM; CLU_004620_3_0_11; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000017984; Chromosome.
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:UP000017984}.
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;  102449 MW;  CD9EA8249B30548B CRC64;
     MTAHRMPLSE LEAGIPFEQR HIGPDQEARA KMLAQVGYGS LDELTAAAVP DVIKNADALD
     LPGARTEAEV LAELRSLAER NQVLGSMIGL GYYGTFTPPV ILRNVMENPA WYTAYTPYQP
     EISQGRLEAL LNFQTVVADL TGLPTSGASL LDEGTAAAEA MALSRRMGKN KKGLFLVDAD
     ALPQTVAVIQ TRAEPTGAEV VVADLSEGIP ADIAAREING VLIQYPGASG AVRDIKPVID
     QAHELGALVT VAADLLALAL LTSPGELGAD IAVGTTQRFG VPMGFGGPHA GYMAVHEKFA
     RSLPGRLVGV SVDADGNKAY RLALQTREQH IRREKATSNI CTAQVLLAVM AGMYAVYHGP
     EGLQTIARRT HRYATILAAG LKAGGVEIVH GAFFDTLTAR VPGKAAGVVA AARQNGVNLH
     LVDADHVSLA CDETTTRAQL GTVWSAFGVE GDTEALDATA EDTLPEALLR TDAYLTHPVF
     HRHRSETAML RYLRKLADRD YALDRGMIPL GSCTMKLNAT TEMEPVTWPE FGQLHPFAPA
     EQAQGYLTLI RELEERLAEV TGYDKVSLQP NAGSQGELAG LLAVRGYHRA CGDEQRVVCL
     IPSSAHGTNA ASAVMAGMKV VVVKTAEDGE IDVEDLRAKI EQYRDELAVL MITYPSTHGV
     FEEHVADICA QVHEAGGQVY VDGANLNALV GLAKPGHFGG DVSHLNLHKT FCIPHGGGGP
     GVGPVAVRAH LAPYLPNHPM QPAAGPETGV GPISAAPWGS AGILPISWAY VRLMGGEGLK
     RATQVAVLSA NYIAKRLEPH YPVLYTGPGG LVAHECIIDL RPLTKATGVS VDDVAKRLID
     YGFHAPTMSF PVAGTLMIEP TESEDITELD RFCDAMIAIR AEIEKVGSGE WPAEDNPLRN
     SPHTAAALGG EWRHAYSRED AVFPAGVSAA DKYWPPVRRI DQAFGDRNLV CSCPPLDAYE
     D
//
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