GCSP2_PSEAE
ID GCSP2_PSEAE Reviewed; 958 AA.
AC Q9HTX7;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) 2;
DE EC=1.4.4.2;
DE AltName: Full=Glycine cleavage system P-protein 2;
DE AltName: Full=Glycine decarboxylase 2;
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) 2;
GN Name=gcvP2; OrderedLocusNames=PA5213;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC [glycine-cleavage complex H protein] + CO2; 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000305}.
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DR EMBL; AE004091; AAG08598.1; -; Genomic_DNA.
DR PIR; E82994; E82994.
DR RefSeq; NP_253900.1; NC_002516.2.
DR RefSeq; WP_003114051.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HTX7; -.
DR SMR; Q9HTX7; -.
DR STRING; 287.DR97_2582; -.
DR PaxDb; Q9HTX7; -.
DR PRIDE; Q9HTX7; -.
DR EnsemblBacteria; AAG08598; AAG08598; PA5213.
DR GeneID; 880606; -.
DR KEGG; pae:PA5213; -.
DR PATRIC; fig|208964.12.peg.5463; -.
DR PseudoCAP; PA5213; -.
DR HOGENOM; CLU_004620_3_2_6; -.
DR InParanoid; Q9HTX7; -.
DR OMA; DEHCHPQ; -.
DR PhylomeDB; Q9HTX7; -.
DR BioCyc; PAER208964:G1FZ6-5332-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR CDD; cd00613; GDC-P; 2.
DR Gene3D; 3.40.640.10; -; 2.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00711; GcvP; 1.
DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR003437; GcvP.
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 PANTHER; PTHR11773; PTHR11773; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR Pfam; PF02347; GDC-P; 1.
DR SUPFAM; SSF53383; SSF53383; 2.
DR TIGRFAMs; TIGR00461; gcvP; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..958
FT /note="Glycine dehydrogenase (decarboxylating) 2"
FT /id="PRO_0000166926"
FT MOD_RES 707
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 958 AA; 104711 MW; 5A2FC2B07691C8DC CRC64;
MSQTPSLAQL QPADAFLRRH LGPDPAEQQA MLAFLGVSTR AELIVQTVPP AIRLNRPLEL
PAALDEQAAL ARLRGYAGLN QRWTSLIGMG YYGTVTPSVI LRNVLENPGW YTAYTPYQPE
IAQGRLEALL NFQQLTIDLT GLDLASASLL DEATAAAEAM ALARRVAKAR SNRFFVDAHC
HPQTVSVLRT RAEAFGFELV VDEPDNLAAH AVFGALLQYP DSRGEIRDLR PLIEALHGQQ
ALACVASDLL ALLLLTPPGE LGADVVLGSA QRFGVPMGYG GPHAAFFATR EGYKRAMPGR
IIGVSRDARG NPALRMALQT REQHIRREKA NSNICTAQVL LANIASLYAV YHGPQELKRI
AQRVQRLTAL LAAGLKSKGL RRLNRHFFDT LTYEVGERQA AILERARAAR VNLRVVDDRR
LALSLDETCD AATLATLFEI FLGAGHGLDV AHLDGGAVAD GIPAVLQRTS AYLQHPVFNA
HHSETEMLRY LRQLEGKDLA LNQAMIPLGS CTMKLNASSE MIPITWPEFA ELHPFVPREQ
AEGYRRMIDE LEAWLRAITG FDAICMQPNS GAQGEYAGLL AIRRYHQSRG DSQRDICLIP
ASAHGTNPAS AIMASMRVVI VECDPRGNVD LDDLRLKAAE AGDRLSCLMI TYPSTHGVYE
EGIGEICEVV HRHGGQVYMD GANLNAQVGL ARPADIGADV SHMNLHKTFC IPHGGGGPGM
GPIGVKRHLA PFVANHPVIR VEGPNPLNDA VSATPWGSAS ILPISWMYIA MMGPQLADAS
EVAILSANYL ANRLDGAFPV LYRGRNERVA HECILDLRPL KAQTGITEED VAKRLMDYGF
HAPTMSFPVP GTLMVEPTES ESKAELDRFV EAMLSIRAEI GKVESGAWPA EDNPLKRAPH
TLADVTGIWQ RPYEIAEAVT PSEHARAFKY WPAVNRVDNV YGDRNLFCAC VPLDDYRE
