ID Q02MP6_PSEAB Unreviewed; 959 AA.
AC Q02MP6;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 29-MAY-2013, entry version 59.
DE RecName: Full=Glycine dehydrogenase [decarboxylating];
DE EC=1.4.4.2;
DE AltName: Full=Glycine cleavage system P-protein;
DE AltName: Full=Glycine decarboxylase;
GN Name=gcvP2; Synonyms=gcvP; OrderedLocusNames=PA14_33000;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
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 (By similarity).
CC -!- SIMILARITY: Belongs to the GcvP family.
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DR EMBL; CP000438; ABJ11629.1; -; Genomic_DNA.
DR RefSeq; YP_790790.1; NC_008463.1.
DR ProteinModelPortal; Q02MP6; -.
DR STRING; 208963.PA14_33000; -.
DR EnsemblBacteria; ABJ11629; ABJ11629; PA14_33000.
DR GeneID; 4380533; -.
DR KEGG; pau:PA14_33000; -.
DR PATRIC; 19851494; VBIPseAer79785_2696.
DR eggNOG; COG1003; -.
DR HOGENOM; HOG000239369; -.
DR KO; K00281; -.
DR OMA; QTMVCDL; -.
DR ProtClustDB; PRK05367; -.
DR BioCyc; PAER208963:GI5K-2676-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; -; 2.
DR HAMAP; MF_00711; GcvP; 1; -.
DR InterPro; IPR020580; GDC-P_N.
DR InterPro; IPR020581; GDC_P.
DR InterPro; IPR003437; GDC_P_homo.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR PANTHER; PTHR11773; PTHR11773; 1.
DR Pfam; PF02347; GDC-P; 2.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 2.
DR TIGRFAMs; TIGR00461; gcvP; 1.
PE 3: Inferred from homology;
KW Complete proteome; Oxidoreductase; Pyridoxal phosphate.
FT MOD_RES 711 711 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 959 AA; 103889 MW; 9599CBAEF1D0C083 CRC64;
MTDNLNLGTI DLGTDDEFIA RHIGPRAADT QAMLQRLGYD SLDTLIGNVI PDSIKGSSVL
DLPAGMGEAE ALASLKAIAA RNRALRSFIG QGYYNCHTPA PILRNLLENP AWYTAYTPYQ
PEISQGRLEA LLNFQTLVSD LSGLPIANAS MLDEATAAAE AMTFCKRLSK NRTSQAFFAS
RHCHPQTLDV LRTRAEPLGI EVVVGDESAI EDFSAYFGAL LQYPTCDGEI VDYRELVSRF
HAVDALVAVA ADLLALTLLT PPGEFGADVA IGSAQRFGVP LGFGGPHAAY FATRDAFKRD
MPGRLVGVSI DRHGKPAYRL AMQTREQHIR REKATSNICT AQVLLANIAS MFAVYHGPQG
LLRIARRTHR LTAILAAGLE RLGVAVEQKH FFDTLSLATG ARTAAIHAKA RAAGINLREI
DAGRLGLSLD ETVRQADVET LWGLLAEEGQ ALPDFAALAA SSGDRLPVEL LRQSAILSHP
IFNRHHSETE LMRYLRKLAD KDLALDRTMI PLGSCTMKLN AASEMIPVTW AEFGNLHPFA
PAEQSEGYRQ LTDELEAMLC SATGYDAVSL QPNAGSQGEY AGLLAIRAYH QSRGDSQRDI
CLIPSSAHGT NPATASMVGM RVVVVACDAR GNVDVEDLRN KASEHKERLA ALMITYPSTH
GVFEEAIREI CAIVHDCGGQ VYIDGANMNA MVGLCAPGKF GGDVSHLNLH KTFCIPHGGG
GPGVGPIGVR AHLAPFLPGH ARGERKEGAV SAAPYGSASI LPITWMYIRM MGGEGLKRAS
EMAILNANYI AHRLEEHYPV LYAGGNGLVA HECILDLRPL KDSSGISVDD VAKRLMDFGF
HAPTMSFPVA GTLMIEPTES ESKAELDRFC DAMIRIREEI RAVERGELDK EDNPLKNAPH
TAAELLGEWN HAYSREQAAY PLASLVEAKY WPPVGRVDNV YGDRNLTCSC PPIEAYSEE
//