GCSP1_PSEAE
ID GCSP1_PSEAE Reviewed; 959 AA.
AC Q9I137;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) 1;
DE EC=1.4.4.2;
DE AltName: Full=Glycine cleavage system P-protein 1;
DE AltName: Full=Glycine decarboxylase 1;
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) 1;
GN Name=gcvP1; OrderedLocusNames=PA2445;
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; AAG05833.1; -; Genomic_DNA.
DR PIR; D83339; D83339.
DR RefSeq; NP_251135.1; NC_002516.2.
DR RefSeq; WP_003115850.1; NZ_QZGE01000041.1.
DR AlphaFoldDB; Q9I137; -.
DR SMR; Q9I137; -.
DR STRING; 287.DR97_5987; -.
DR PaxDb; Q9I137; -.
DR PRIDE; Q9I137; -.
DR EnsemblBacteria; AAG05833; AAG05833; PA2445.
DR GeneID; 882927; -.
DR KEGG; pae:PA2445; -.
DR PATRIC; fig|208964.12.peg.2558; -.
DR PseudoCAP; PA2445; -.
DR HOGENOM; CLU_004620_3_2_6; -.
DR InParanoid; Q9I137; -.
DR OMA; CVPMSEY; -.
DR PhylomeDB; Q9I137; -.
DR BioCyc; PAER208964:G1FZ6-2482-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: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; 1.
DR Gene3D; 3.40.640.10; -; 2.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00711; GcvP; 1.
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; PF02347; GDC-P; 2.
DR SUPFAM; SSF53383; SSF53383; 2.
DR TIGRFAMs; TIGR00461; gcvP; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..959
FT /note="Glycine dehydrogenase (decarboxylating) 1"
FT /id="PRO_0000166925"
FT MOD_RES 711
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 959 AA; 103919 MW; B8AAB1799210285D CRC64;
MTDNLNLGAI DLGTDDEFIA RHIGPRAADT QAMLQRLGYD SLDTLIGNVI PDSIKGSSVL
DLPAGMGEAE ALASLKAIAA RNRALRSFIG QGYYNCHTPA PILRNLLENP AWYTAYTPYQ
PEISQGRLEA LLNFQTLVSD LSGLPIANAS MLDEATAAAE AMTFCKRLSK NRTSQAFFAS
RHCHPQTLDV LRTRAEPLGI EVVVGDESTI EDFSAYFGAL LQYPTCDGEI VDYRELVSRF
HAVDALVAVA ADLLALTLLT PPGEFGADVA IGSAQRFGVP LGFGGPHAAY FATRDAFKRD
MPGRLVGVSI DRHGKPAYRL AMQTREQHIR REKATSNICT AQVLLANIAS MFAVYHGPQG
LLRIARRTHR LTAILAAGLE RLGVAVEQKH FFDTLSLATG ARTAAIHAKA RAAGINLREI
DAGRLGLSLD ETVRQTDVET 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
