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   27-MAR-2024, entry version 123.
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; 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; 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; 208964.PA5213; -.
DR   PaxDb; 208964-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   OrthoDB; 9801272at2; -.
DR   PhylomeDB; Q9HTX7; -.
DR   BioCyc; PAER208964:G1FZ6-5332-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; 2.
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:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
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
//