ID D5ZTX6_STRV1 Unreviewed; 961 AA.
AC D5ZTX6;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=SSFG_05992 {ECO:0000313|EMBL:EFE70749.2};
OS Streptomyces viridosporus (strain ATCC 14672 / DSM 40746 / JCM 4963 / KCTC
OS 9882 / NRRL B-12104 / FH 1290) (Streptomyces ghanaensis).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=566461 {ECO:0000313|EMBL:EFE70749.2, ECO:0000313|Proteomes:UP000003824};
RN [1] {ECO:0000313|Proteomes:UP000003824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14672 / DSM 40746 / JCM 4963 / KCTC 9882 / NRRL B-12104 /
RC FH 1290 {ECO:0000313|Proteomes:UP000003824};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M.,
RA Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces ghanaensis ATCC 14672.";
RL Submitted (DEC-2008) 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}.
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DR EMBL; DS999641; EFE70749.2; -; Genomic_DNA.
DR RefSeq; WP_004990893.1; NZ_DS999641.1.
DR AlphaFoldDB; D5ZTX6; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR Proteomes; UP000003824; 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}.
FT DOMAIN 19..446
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 453..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 REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 102757 MW; C955AC7D0C90D247 CRC64;
MTVHRTPLSE LEQGTPFEQR HIGPDHEARA KMLAQVGYGS LDELTAAAVP DVIKNADALD
LPGARSEAEV LAELRSLAGR NEVLGSMIGL GYYGTFTPPV ILRNVMENPA WYTAYTPYQP
EISQGRLEAL LNFQTTVAEL TGLPTSGASL LDEGTAAAEA MALSRRMGKN KKGLFLVDAD
ALPQTIAVIE TRAEPTGVEV VVADLSEGIP AEVAEREING VLIQYPGASG AVRDIKPVID
RAHELGALVT VAADLLALTL LKSPGELGAD IAVGTTQRFG VPMGFGGPHA GYMAVQEKMA
RSLPGRLVGV SVDADGHQAY RLALQTREQH IRREKATSNI CTAQVLLAVM AGMYAVYHGP
QGLRTIARRT HRYAAVLAEG LRAGGAEIVH ASYFDTLTVR VPGRAAEVVA AARDRGVNLR
LVDADHVSIA CDETTTRDRL AAVWGAFGVE GDVEALDAVA EDALPDALLR TDEYLTHPVF
HQHRSETAML RYLRRLADRD YALDRGMIPL GSCTMKLNAT TEMEPITWPE FGQLHPFAPA
EQAQGYLTLI HELEERLAEV TGYDKVSLQP NAGSQGELAG LLAVRGYHRA NGDAQRTVCL
IPSSAHGTNA ASAVMAGMKV VVVRTAENGE VDVEDLRAKI EQYRDELAVL MITYPSTHGV
FEEHVADICA QVHEAGGQVY VDGANLNALV GLAKPGHFGG DVSHLNLHKT FCIPHGGGGP
GVGPVGVRAH LAPYLPNHPL QPEAGPETGV GPISAAPWGS AGILPISWAY VRLMGGEGLK
RATQVAVLSA NYIAKRLEPH YPVLYTGPGG LVAHECIIDL RPLTKATGVS VDDVAKRLID
YGFHAPTMSF PVAGTLMIEP TESEDLAEID RFCEAMIAIR AEIEKVGSGA WPADDNPLRN
APHTAAALGG EWEHAYGREE AVFPAGVSAA DKYWPPVRRI DQAFGDRNLV CSCPPLDAYE
D
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