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   27-MAR-2024, entry version 118.
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; Pseudomonadota; 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 /
RC   1C / 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=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   -!- 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; 208964.PA2445; -.
DR   PaxDb; 208964-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   OrthoDB; 9801272at2; -.
DR   PhylomeDB; Q9I137; -.
DR   BioCyc; PAER208964:G1FZ6-2482-MONOMER; -.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
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; 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
//