ID E6TX01_BACCJ Unreviewed; 488 AA.
AC E6TX01;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 01-MAY-2013, entry version 17.
DE RecName: Full=Probable glycine dehydrogenase [decarboxylating] subunit 2;
DE EC=1.4.4.2;
DE AltName: Full=Glycine cleavage system P-protein subunit 2;
DE AltName: Full=Glycine decarboxylase subunit 2;
GN Name=gcvPB; OrderedLocusNames=Bcell_1688;
OS Bacillus cellulosilyticus (strain ATCC 21833 / DSM 2522 / FERM P-1141
OS / JCM 9156 / N-4).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=649639;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21833 / DSM 2522 / FERM P-1141 / JCM 9156 / N-4;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Brumm P., Mead D., Woyke T.;
RT "Complete sequence of Bacillus cellulosilyticus DSM 2522.";
RL Submitted (DEC-2010) 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
CC through its pyridoxal phosphate cofactor; CO(2) is released and
CC the remaining methylamine moiety is then transferred to the
CC lipoamide cofactor of the H protein (By similarity).
CC -!- CATALYTIC ACTIVITY: Glycine + H-protein-lipoyllysine = H-protein-
CC S-aminomethyldihydrolipoyllysine + CO(2).
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins:
CC P, T, L and H. In this organism, the P 'protein' is a heterodimer
CC of two subunits (By similarity).
CC -!- SIMILARITY: Belongs to the GcvP family. C-terminal subunit
CC subfamily.
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DR EMBL; CP002394; ADU29951.1; -; Genomic_DNA.
DR RefSeq; YP_004094682.1; NC_014829.1.
DR ProteinModelPortal; E6TX01; -.
DR EnsemblBacteria; ADU29951; ADU29951; Bcell_1688.
DR GeneID; 10088251; -.
DR KEGG; bco:Bcell_1688; -.
DR PATRIC; 45159309; VBIBacCel7049_1738.
DR HOGENOM; HOG000239368; -.
DR KO; K00283; -.
DR BioCyc; BCEL649639:GHTT-1759-MONOMER; -.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:HAMAP.
DR Gene3D; 3.40.640.10; -; 3.
DR HAMAP; MF_00713; GcvPB; 1; -.
DR InterPro; IPR020580; GDC-P_N.
DR InterPro; IPR020581; GDC_P.
DR InterPro; IPR023012; GDC_P_su2.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR PANTHER; PTHR11773; PTHR11773; 1.
DR Pfam; PF02347; GDC-P; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
PE 3: Inferred from homology;
KW Complete proteome; Oxidoreductase; Pyridoxal phosphate.
FT MOD_RES 274 274 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 488 AA; 54547 MW; 4E68EE6DED97E524 CRC64;
MIHQQDQALI FEISKEGRIG HSLPEMDVPE VALDELIPSQ FQREEAAELP EVSELQLVRH
YTALSRRNHG VDSGFYPLGS CTMKYNPKIN EDVARYPGFA HIHPYQAEST IQGALELMYH
LQNSLAEITG MDEVTLQPAA GAHGEWTGLM MIRAFHEANG DTHRTKVIVP DSAHGTNPAS
ATVAGFESVT VRSNEKGLVD LDHLKEVVGE DTAALMLTNP NTLGLFEEQI VEMAEIVHNA
GGKLYYDGAN SNAILGITRP GDMGFDVVHL NLHKTFTTPH GGGGPGSGPV GVKKDLIPFL
PKPTVVKDGE TYRFEYNLPQ SIGRVKPYYG NFGINVRAYT YIRTMGPEGL RQVSEHAVLN
ANYMFRRLQP YYDAPYTQHC KHEFVLSGRR QKRLGVRTLD IAKRLLDFGY HPPTIYFPLN
VEECLMIEPT ETESKETLDE FIDAMIQIAK EAEETPEIVQ EAPHHTVIDR LDETTAARKP
VLRYTKED
//
