ID S3XYD7_9MICO Unreviewed; 997 AA.
AC S3XYD7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=HMPREF1484_01386 {ECO:0000313|EMBL:EPH15749.1};
OS Dermabacter sp. HFH0086.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Dermabacter.
OX NCBI_TaxID=1203568 {ECO:0000313|EMBL:EPH15749.1, ECO:0000313|Proteomes:UP000014577};
RN [1] {ECO:0000313|EMBL:EPH15749.1, ECO:0000313|Proteomes:UP000014577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HFH0086 {ECO:0000313|EMBL:EPH15749.1,
RC ECO:0000313|Proteomes:UP000014577};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dermabacter sp. HFH0086.";
RL Submitted (MAY-2013) 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:EPH15749.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ATFO01000007; EPH15749.1; -; Genomic_DNA.
DR AlphaFoldDB; S3XYD7; -.
DR STRING; 1203568.HMPREF1484_01386; -.
DR PATRIC; fig|1203568.3.peg.1361; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_1_1_11; -.
DR Proteomes; UP000014577; Unassembled WGS sequence.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
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 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:UP000014577}.
FT DOMAIN 23..451
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 487..746
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 799..920
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 718
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 997 AA; 107337 MW; 2E98C0D48F4DEA90 CRC64;
MSEHHSNVAV DNSAIDGLHS FVRRHVGTAS EDQKRMLEAL GLDSLGALLE KAVPGTILLD
EGLDSLLPEG ASEAEALEEL RALAKKNTVK RSLIGHGYYG TYTPSVIQRN ILENPAWYTA
YTPYQPEISQ GRLEALLNYQ TMIGDLTGLE IANSSMLDEA TAAAEAMLLA RRAARGNKSN
VFLVDTDVLP STRAVLGGRA EAVGIELKDV DFANDGAPSG EYFGALVQYP GASGRVWDPR
DVIAAVQANK AKAIVAADLL ALTLLASPGE LGADVAVGNS QRFGVPLGFG GPHAGYMAVS
KGLERQIPGR LVGISLDAEG NPAYRLALQT REQHIRREKA TSNICTAQVL LAVMASMYAV
YHGPEGLKQI ASEVAGRTAA LAAWLTSNGF QLKHETFFDT LEVTVNGKAE DIARAFDDRG
ILVAHPDADT VHISLDETVT PSALSEIIEV FSEFSPSHVG DVAFDEWAQP GETWGELART
SSFLEAPVFN SFRSETAMMR YLRRLADKDY ALDRGMIPLG SCTMKLNAAT EMAAVTWPEF
NAIHPSAPAS DVQGYVELIT QLETWLADVT GYDTVSLQPN AGSQGEYAGL LAIRAYHASR
GESARTVCLV PSSAHGTNAA SAVLAGLRVV VVASDANGNV DLDDLKQKIK DHADELACIM
ITYPSTHGVY ESEVRTITQL VHDAGGQVYV DGANLNALLE VAKPGEFGGD VSHLNLHKTF
CIPHGGGGPG VGPVAAKAHL APFLPGHPDM QNAEHPVIGG ADRAHGGAPV SQAPYGSPSI
LPIPWTYIRL MGAKGLRHAT ASAVLAANYM AKRLSEKFEI LYRGENGLVA HECIVDLRPF
TDRTGITVDD VAKRLIDYGF HAPTMSFPVA GTLMIEPTES EDLWEIERFI LAMHRIADEA
EKVVSGEWPK DDNPLVNAPH TAYSVAREDW DHPYSRDEAV YPGVNAASEA GYDPDFHMTK
QMQYQAKYWP PVRRIDQAYG DRNLVCSCQP LDAYEQG
//
