LDCA_PSEAE
ID LDCA_PSEAE Reviewed; 751 AA.
AC Q9I2S7;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Lysine decarboxylase LdcA {ECO:0000303|PubMed:20833801};
DE EC=4.1.1.18 {ECO:0000269|PubMed:20833801};
GN Name=ldcA {ECO:0000303|PubMed:20833801}; OrderedLocusNames=PA1818;
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).
RN [2]
RP FUNCTION, INDUCTION BY ARGININE, DISRUPTION PHENOTYPE, AND CATALYTIC
RP ACTIVITY.
RX PubMed=20833801; DOI=10.1128/jb.00673-10;
RA Chou H.T., Hegazy M., Lu C.D.;
RT "L-lysine catabolism is controlled by L-arginine and ArgR in Pseudomonas
RT aeruginosa PAO1.";
RL J. Bacteriol. 192:5874-5880(2010).
RN [3]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=31653338; DOI=10.1016/j.str.2019.10.003;
RA Kandiah E., Carriel D., Garcia P.S., Felix J., Banzhaf M., Kritikos G.,
RA Bacia-Verloop M., Brochier-Armanet C., Elsen S., Gutsche I.;
RT "Structure, Function, and Evolution of the Pseudomonas aeruginosa Lysine
RT Decarboxylase LdcA.";
RL Structure 0:0-0(2019).
CC -!- FUNCTION: Plays an essential role in lysine utilization by acting as a
CC lysine decarboxylase. {ECO:0000269|PubMed:20833801,
CC ECO:0000269|PubMed:31653338}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-lysine = cadaverine + CO2; Xref=Rhea:RHEA:22352,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:58384; EC=4.1.1.18;
CC Evidence={ECO:0000269|PubMed:20833801};
CC -!- SUBUNIT: Homodecamer. {ECO:0000269|PubMed:31653338}.
CC -!- INDUCTION: Transcriptionally regulated by ArgR in response to arginine
CC but not lysine showing a tight connection of lysine catabolism to the
CC arginine regulatory network. {ECO:0000269|PubMed:20833801}.
CC -!- DISRUPTION PHENOTYPE: Loss of growth on lysine as sole carbon source
CC (PubMed:20833801). Inactivation leads also to a decrease of virulence
CC showing the importance of LdcA involvement in polyamine homeostasis
CC during infection of the host (PubMed:31653338).
CC {ECO:0000269|PubMed:20833801, ECO:0000269|PubMed:31653338}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG05207.1; -; Genomic_DNA.
DR PIR; D83418; D83418.
DR RefSeq; NP_250509.1; NC_002516.2.
DR RefSeq; WP_003113592.1; NZ_QZGE01000003.1.
DR PDB; 6Q6I; EM; 3.70 A; A=1-751.
DR PDBsum; 6Q6I; -.
DR AlphaFoldDB; Q9I2S7; -.
DR SMR; Q9I2S7; -.
DR STRING; 287.DR97_61; -.
DR PaxDb; Q9I2S7; -.
DR PRIDE; Q9I2S7; -.
DR EnsemblBacteria; AAG05207; AAG05207; PA1818.
DR GeneID; 878596; -.
DR KEGG; pae:PA1818; -.
DR PATRIC; fig|208964.12.peg.1888; -.
DR PseudoCAP; PA1818; -.
DR HOGENOM; CLU_014292_3_0_6; -.
DR InParanoid; Q9I2S7; -.
DR OMA; WSTLLTE; -.
DR PhylomeDB; Q9I2S7; -.
DR BioCyc; PAER208964:G1FZ6-1856-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0008923; F:lysine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR CDD; cd00615; Orn_deC_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005308; OKR_de-COase_N.
DR InterPro; IPR011193; Orn/lys/arg_de-COase.
DR InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF01276; OKR_DC_1; 1.
DR Pfam; PF03711; OKR_DC_1_C; 1.
DR Pfam; PF03709; OKR_DC_1_N; 1.
DR PIRSF; PIRSF009393; Orn_decarb; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR SUPFAM; SSF55904; SSF55904; 1.
DR PROSITE; PS00703; OKR_DC_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Decarboxylase; Lyase; Pyridoxal phosphate;
KW Reference proteome; Virulence.
FT CHAIN 1..751
FT /note="Lysine decarboxylase LdcA"
FT /id="PRO_0000448879"
SQ SEQUENCE 751 AA; 82757 MW; 4A32C928AA8468A1 CRC64;
MYKDLKFPVL IVHRDIKADT VAGERVRGIA HELEQDGFSI LSTASSAEGR IVASTHHGLA
CILVAAEGAG ENQRLLQDVV ELIRVARVRA PQLPIFALGE QVTIENAPAE SMADLHQLRG
ILYLFEDTVP FLARQVARAA RNYLAGLLPP FFRALVEHTA QSNYSWHTPG HGGGVAYRKS
PVGQAFHQFF GENTLRSDLS VSVPELGSLL DHTGPLAEAE DRAARNFGAD HTFFVINGTS
TANKIVWHSM VGREDLVLVD RNCHKSILHS IIMTGAIPLY LTPERNELGI IGPIPLSEFS
KQSIAAKIAA SPLARGREPK VKLAVVTNST YDGLCYNAEL IKQTLGDSVE VLHFDEAWYA
YAAFHEFYDG RYGMGTSRSE EGPLVFATHS THKMLAAFSQ ASMIHVQDGG TRKLDVARFN
EAFMMHISTS PQYGIIASLD VASAMMEGPA GRSLIQETFD EALSFRRALA NVRQNLDRND
WWFGVWQPEQ VEGTDQVGTH DWVLEPSADW HGFGDIAEDY VLLDPIKVTL TTPGLSAGGK
LSEQGIPAAI VSRFLWERGL VVEKTGLYSF LVLFSMGITK GKWSTLVTEL LEFKRCYDAN
LPLLDVLPSV AQAGGKRYNG VGLRDLSDAM HASYRDNATA KAMKRMYTVL PEVAMRPSEA
YDKLVRGEVE AVPIARLEGR IAAVMLVPYP PGIPLIMPGE RFTEATRSIL DYLEFARTFE
RAFPGFDSDV HGLQHQDGPS GRCYTVECIK E
