ACEA_PSEAE
ID ACEA_PSEAE Reviewed; 531 AA.
AC Q9I0K4;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Isocitrate lyase {ECO:0000250|UniProtKB:P0A9G6};
DE Short=ICL {ECO:0000250|UniProtKB:P0A9G6};
DE EC=4.1.3.1 {ECO:0000250|UniProtKB:P0A9G6};
DE AltName: Full=Isocitrase {ECO:0000250|UniProtKB:P0A9G6};
DE AltName: Full=Isocitratase {ECO:0000250|UniProtKB:P0A9G6};
GN OrderedLocusNames=PA2634;
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 PROTEIN SEQUENCE OF 110-138; 144-156; 245-260; 318-325; 393-404; 414-426
RP AND 468-480.
RC STRAIN=ATCC 33467 / type 1 smooth;
RA Liddor M.;
RT "Biofouling in water treatment systems: effect of membrane properties on
RT biofilm formation.";
RL Thesis (2005), Ben-Gurion University, Israel.
CC -!- FUNCTION: Involved in the metabolic adaptation in response to
CC environmental changes. Catalyzes the reversible formation of succinate
CC and glyoxylate from isocitrate, a key step of the glyoxylate cycle,
CC which operates as an anaplerotic route for replenishing the
CC tricarboxylic acid cycle during growth on fatty acid substrates.
CC {ECO:0000250|UniProtKB:P0A9G6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate = glyoxylate + succinate;
CC Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:36655; EC=4.1.3.1;
CC Evidence={ECO:0000250|UniProtKB:P0A9G6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A9G6};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 1/2. {ECO:0000250|UniProtKB:P0A9G6}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A9G6}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG06022.1; -; Genomic_DNA.
DR PIR; G83315; G83315.
DR RefSeq; NP_251324.1; NC_002516.2.
DR RefSeq; WP_003113373.1; NZ_QZGE01000008.1.
DR PDB; 6G1O; X-ray; 1.88 A; A=1-486.
DR PDBsum; 6G1O; -.
DR AlphaFoldDB; Q9I0K4; -.
DR SMR; Q9I0K4; -.
DR STRING; 287.DR97_5328; -.
DR PaxDb; Q9I0K4; -.
DR PRIDE; Q9I0K4; -.
DR EnsemblBacteria; AAG06022; AAG06022; PA2634.
DR GeneID; 882341; -.
DR KEGG; pae:PA2634; -.
DR PATRIC; fig|208964.12.peg.2756; -.
DR PseudoCAP; PA2634; -.
DR HOGENOM; CLU_038243_0_0_6; -.
DR InParanoid; Q9I0K4; -.
DR OMA; ARFQWDM; -.
DR PhylomeDB; Q9I0K4; -.
DR BioCyc; PAER208964:G1FZ6-2674-MON; -.
DR BRENDA; 4.1.3.1; 5087.
DR UniPathway; UPA00703; UER00719.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0004451; F:isocitrate lyase activity; IDA:PseudoCAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniPathway.
DR GO; GO:1900232; P:negative regulation of single-species biofilm formation on inanimate substrate; IMP:PseudoCAP.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR006254; Isocitrate_lyase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR21631; PTHR21631; 1.
DR Pfam; PF00463; ICL; 3.
DR PIRSF; PIRSF001362; Isocit_lyase; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glyoxylate bypass; Lyase;
KW Magnesium; Metal-binding; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..531
FT /note="Isocitrate lyase"
FT /id="PRO_0000068780"
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A9G6"
FT BINDING 101..103
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A9G6"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A9G6"
FT BINDING 223..224
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 380..384
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 451
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 42..62
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 124..157
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 233..249
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 281..287
FT /evidence="ECO:0007829|PDB:6G1O"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 330..343
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 358..369
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 387..400
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 423..442
FT /evidence="ECO:0007829|PDB:6G1O"
FT STRAND 445..452
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 453..469
FT /evidence="ECO:0007829|PDB:6G1O"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:6G1O"
FT HELIX 475..481
FT /evidence="ECO:0007829|PDB:6G1O"
FT TURN 482..485
FT /evidence="ECO:0007829|PDB:6G1O"
SQ SEQUENCE 531 AA; 58887 MW; F45A4ECDA3F220CA CRC64;
MSAYQNEIKA VAALKEKNGS SWSAINPEYA ARMRIQNRFK TGLDIAKYTA AIMRKDMAEY
DADSSVYTQS LGCWHGFIGQ QKLISIKKHL KTTNKRYLYL SGWMVAALRS DFGPLPDQSM
HEKTAVSGLI EELYTFLRQA DARELDLLFT GLDAARAAGD KAKEAELLAQ IDNFETHVVP
IIADIDAGFG NAEATYLLAK KMIEAGACCI QIENQVSDEK QCGHQDGKVT VPHIDFLAKI
NAVRYAFLEL GVDDGVIVAR TDSLGAGLTK QIAVTNEPGD LGDLYNSFLD CEEISESELG
NGDVVIKREG KLLRPKRLAS NLFQFRKGTG EDRCVLDCIT SLQNGADLLW IETEKPHVGQ
IKAMVDRIRE VIPNAKLVYN NSPSFNWTLN FRQQVFDAFV AEGKDVSAYD RNKLMSVEYD
DTELAKVADE KIRTFQRDGS AHAGIFHHLI TLPTYHTAAL STDNLAKGYF ADEGMLAYVK
GVQRQELRQG IACVKHQNMA GSDIGDNHKE YFAGEAALKA SGKDNTMNQF H
