ACNB_PSEAE
ID ACNB_PSEAE Reviewed; 869 AA.
AC Q9I2V5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Aconitate hydratase B {ECO:0000250|UniProtKB:P36683};
DE Short=ACN {ECO:0000250|UniProtKB:P36683};
DE Short=Aconitase {ECO:0000250|UniProtKB:P36683};
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:P36683};
DE AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000250|UniProtKB:P36683};
DE AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000250|UniProtKB:P36683};
DE AltName: Full=2-methyl-cis-aconitate hydratase {ECO:0000250|UniProtKB:P36683};
DE EC=4.2.1.99 {ECO:0000250|UniProtKB:P36683};
DE AltName: Full=Iron-responsive protein-like {ECO:0000250|UniProtKB:P36683};
DE Short=IRP-like {ECO:0000250|UniProtKB:P36683};
DE AltName: Full=RNA-binding protein {ECO:0000250|UniProtKB:P36683};
GN Name=acnB; OrderedLocusNames=PA1787;
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: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the tricarboxylic acid (TCA)(acetyl degradation route) and probably
CC via the 2-methylcitrate cycle I (propionate degradation route).
CC Catalyzes the reversible isomerization of citrate to isocitrate via
CC cis-aconitate. Catalyzes the hydration of 2-methyl-cis-aconitate to
CC yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a
CC RNA-binding regulatory protein. {ECO:0000250|UniProtKB:P36683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:P36683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC Evidence={ECO:0000250|UniProtKB:P36683};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P36683};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P36683};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000250|UniProtKB:P36683}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000250|UniProtKB:P36683}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P36683}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG05176.1; -; Genomic_DNA.
DR PIR; G83422; G83422.
DR RefSeq; NP_250478.1; NC_002516.2.
DR RefSeq; WP_003087875.1; NZ_QZGE01000003.1.
DR AlphaFoldDB; Q9I2V5; -.
DR SMR; Q9I2V5; -.
DR STRING; 287.DR97_99; -.
DR PaxDb; Q9I2V5; -.
DR PRIDE; Q9I2V5; -.
DR EnsemblBacteria; AAG05176; AAG05176; PA1787.
DR GeneID; 879984; -.
DR KEGG; pae:PA1787; -.
DR PATRIC; fig|208964.12.peg.1853; -.
DR PseudoCAP; PA1787; -.
DR HOGENOM; CLU_016536_0_0_6; -.
DR InParanoid; Q9I2V5; -.
DR OMA; QDTTGAM; -.
DR PhylomeDB; Q9I2V5; -.
DR BioCyc; PAER208964:G1FZ6-1819-MON; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0003994; F:aconitate hydratase activity; ISS:UniProtKB.
DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; ISS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB.
DR CDD; cd01576; AcnB_Swivel; 1.
DR Gene3D; 1.25.40.310; -; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR Gene3D; 3.40.1060.10; -; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR004406; Aconitase_B.
DR InterPro; IPR015933; Aconitase_B_HEAT-like_dom.
DR InterPro; IPR036288; Aconitase_B_HEAT-like_dom_sf.
DR InterPro; IPR015929; Aconitase_B_swivel.
DR InterPro; IPR015932; Aconitase_dom2.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF06434; Aconitase_2_N; 1.
DR Pfam; PF11791; Aconitase_B_N; 1.
DR PIRSF; PIRSF036687; AcnB; 1.
DR SUPFAM; SSF53732; SSF53732; 1.
DR SUPFAM; SSF74778; SSF74778; 1.
DR TIGRFAMs; TIGR00117; acnB; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome;
KW RNA-binding; Tricarboxylic acid cycle.
FT CHAIN 1..869
FT /note="Aconitate hydratase B"
FT /id="PRO_0000287740"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 244..246
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 417..419
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 501
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 713
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 772
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 775
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 794
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 799
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 869 AA; 93628 MW; D8026242DFAED72B CRC64;
MLEAYRKHVE ERAAQGVVPQ PLNAEQTAGL VELLKNPPAG EEEFLLDLIT NRVPPGVDEA
AYVKAGFLSA IVKGEATSPL IDKQRAAELL GTMQGGYNIA TLVELLDDAE LANTAAEQLK
HTLLMFDAFH DVAERAKKGN AAAKSVLQSW ADGEWFKAKP EVPEKLTLTV FKVPGETNTD
DLSPAPDAWS RPDIPLHALA MLKMARDGIE PVQPGSVGPL KQIEAVKAKG FPVAYVGDVV
GTGSSRKSAT NSVLWFFGDD IPFVPNKRAG GFCFGTKIAP IFYNTMEDAG ALPIEFDCTN
LAMGDVIDVY PYEGKVVRHD SGEVVTTFEL KTPVLLDEVR AGGRIPLIVG RGLTEKARAE
LGLGASDLFR KPEAPADSGK GFTLAQKMVG RACGLPEGQG VRPGTYCEPK MTTVGSQDTT
GPMTRDELKD LACLGFSADL VMQSFCHTAA YPKPIDVKTH HTLPDFIMTR GGVSLRPGDG
IIHSWLNRML LPDTVGTGGD SHTRFPIGIS FPAGSGLVAF AAATGVMPLD MPESVLVRFK
GKLQPGITLR DLVHAIPYYA IQQGLLTVEK KGKKNIFSGR ILEIEGLNDL TVEQAFELSD
ASAERSAAGC TIKLPEQAIA EYLKSNITLL RWMIGEGYGD PRTLERRAQA MEAWLAKPEL
LEADKDAEYA AVIEIDLADV KEPVLCAPND PDDARLLSSV QGRKIDEVFI GSCMTNIGHF
RAAGKLLDKV KGGIPTRLWL APPTKMDAHQ LTEEGYYGIY GKAGARMEMP GCSLCMGNQA
RVQTGSTVVS TSTRNFPNRL GDATDVFLAS AELAAVSSIL GKLPTVEEYM AYAKDIDSMA
ADVYRYLSFD QIAEFREAAA NAKIPVVQA
