ID   AIS_PSESP               Reviewed;         262 AA.
AC   A0A0A1H8I4;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Aconitate isomerase {ECO:0000303|PubMed:26293748};
DE            Short=AI {ECO:0000303|PubMed:26293748};
DE            EC=5.3.3.7 {ECO:0000269|PubMed:26293748};
DE   Flags: Precursor;
GN   Name=ais {ECO:0000312|EMBL:BAP90747.1};
OS   Pseudomonas sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=306;
RN   [1] {ECO:0000312|EMBL:BAP90747.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-37, FUNCTION,
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, BIOTECHNOLOGY, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=WU-0701 {ECO:0000312|EMBL:BAP90747.1};
RX   PubMed=26293748; DOI=10.1111/febs.13494;
RA   Yuhara K., Yonehara H., Hattori T., Kobayashi K., Kirimura K.;
RT   "Enzymatic characterization and gene identification of aconitate isomerase,
RT   an enzyme involved in assimilation of trans-aconitic acid, from Pseudomonas
RT   sp. WU-0701.";
RL   FEBS J. 282:4257-4267(2015).
CC   -!- FUNCTION: Involved in assimilation of trans-aconitic acid. Preference
CC       for cis-aconitic acid is 14-fold higher than for trans-aconitic acid.
CC       Not active on intermediates of tricarboxylic acid (TCA) cycle including
CC       citric acid, succinic acid, fumaric acid, and 2-oxoglutaric acid or on
CC       other dicarboxilic acids including itaconic acid, formic acid,
CC       citraconic acid or maleic acid. {ECO:0000269|PubMed:26293748}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=trans-aconitate = cis-aconitate; Xref=Rhea:RHEA:17265,
CC         ChEBI:CHEBI:15708, ChEBI:CHEBI:16383; EC=5.3.3.7;
CC         Evidence={ECO:0000269|PubMed:26293748};
CC   -!- ACTIVITY REGULATION: Activated more than 1.5 fold by Ca(2+), Mg(2+),
CC       Mn(2+), Ni(2+), Fe(2+), DDT and 1,10-phenanthroline. Strongly inhibited
CC       by Ag(+) and Hg(+). Inhibited by addition of 20% (v/v) glycerol. No
CC       effect by addition of NADH or NADPH. {ECO:0000269|PubMed:26293748}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.9 mM for cis-aconitic acid {ECO:0000269|PubMed:26293748};
CC         KM=80 mM for trans-aconitic acid {ECO:0000269|PubMed:26293748};
CC         Note=kcat and kcat/KM are 4500 sec(-1) and 760 sec(-1) mM(-1),
CC         respectively for cis-aconitic acid. kcat and kcat/KM are 15000 sec(-
CC         1) and 190 sec(-1) mM(-1), respectively for trans-aconitic acid.
CC         {ECO:0000269|PubMed:26293748};
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:26293748};
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.
CC         {ECO:0000269|PubMed:26293748};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26293748}.
CC   -!- BIOTECHNOLOGY: May be useful in development of a bioprocess for
CC       effective production of trans-aconitic acid.
CC       {ECO:0000303|PubMed:26293748}.
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; LC010980; BAP90747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1H8I4; -.
DR   SMR; A0A0A1H8I4; -.
DR   KEGG; ag:BAP90747; -.
DR   BRENDA; 5.3.3.7; 16133.
DR   SABIO-RK; A0A0A1H8I4; -.
DR   GO; GO:0047614; F:aconitate delta-isomerase activity; IDA:UniProtKB.
DR   GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
DR   GO; GO:0071281; P:cellular response to iron ion; IDA:UniProtKB.
DR   GO; GO:0071286; P:cellular response to magnesium ion; IDA:UniProtKB.
DR   GO; GO:0071287; P:cellular response to manganese ion; IDA:UniProtKB.
DR   GO; GO:0071289; P:cellular response to nickel ion; IDA:UniProtKB.
DR   GO; GO:0071292; P:cellular response to silver ion; IDA:UniProtKB.
DR   GO; GO:0046680; P:response to DDT; IDA:UniProtKB.
DR   GO; GO:0046689; P:response to mercury ion; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Isomerase; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:26293748"
FT   CHAIN           23..262
FT                   /note="Aconitate isomerase"
FT                   /id="PRO_0000434591"
SQ   SEQUENCE   262 AA;  27449 MW;  70EB60B3E26DAB16 CRC64;
     MFPRLPTLAL GALLLASTPL LAAQPVTTLT VLSSGGIMGT IREVAPAYEK ATGVKLDIAA
     APSMGDTPQA IPNRLARNEP ADVVLMVGSA LDKLVASGQV AKDSRVDLGQ SFIAMAVRQG
     APKPDISNMD AFKQTLEKAQ SVAYSDSASG VYLSRILFPR MQLDKSFMAK ARMIPAEPVG
     AVVARGEAQL GFQQLSELKA VPGIDIVGLI PDQAQKMTLY SGAMVSKSQH PEAARALLQY
     LASKDAAKAI EDSGLKPVPA QP