ID A0A0J8YQM1_9GAMM Unreviewed; 839 AA.
AC A0A0J8YQM1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Aconitate hydratase B {ECO:0000256|ARBA:ARBA00019379, ECO:0000256|PIRNR:PIRNR036687};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|PIRNR:PIRNR036687};
DE EC=4.2.1.99 {ECO:0000256|ARBA:ARBA00013250, ECO:0000256|PIRNR:PIRNR036687};
DE AltName: Full=2-methylisocitrate dehydratase {ECO:0000256|PIRNR:PIRNR036687};
GN ORFNames=AI28_14505 {ECO:0000313|EMBL:KMV72136.1};
OS bacteria symbiont BFo1 of Frankliniella occidentalis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae.
OX NCBI_TaxID=1628855 {ECO:0000313|EMBL:KMV72136.1, ECO:0000313|Proteomes:UP000037152};
RN [1] {ECO:0000313|EMBL:KMV72136.1, ECO:0000313|Proteomes:UP000037152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFo1 {ECO:0000313|EMBL:KMV72136.1,
RC ECO:0000313|Proteomes:UP000037152};
RA Facey P.D., Hitchings M.D., Hegarty M.J., Pachebat J.A., Morgan L.V.,
RA Hoeppner J.E., Whitten M.A., Dyson P.J., Del Sol R.;
RT "The draft genomes, genome evolution and classification of BFo1 and BFo2
RT two insect symbionts isolated from Western Flower Thrips (Frankliniella
RT occidentalis [Pergande]).";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000118,
CC ECO:0000256|PIRNR:PIRNR036687};
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:0000256|ARBA:ARBA00023501,
CC ECO:0000256|PIRNR:PIRNR036687};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRSR:PIRSR036687-1};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000256|PIRSR:PIRSR036687-1};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717,
CC ECO:0000256|PIRNR:PIRNR036687}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000256|ARBA:ARBA00005026}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|PIRNR:PIRNR036687}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMV72136.1}.
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; JMSO01000044; KMV72136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8YQM1; -.
DR STRING; 1628855.WB66_04145; -.
DR PATRIC; fig|1628855.3.peg.2932; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000037152; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01581; AcnB; 1.
DR CDD; cd01576; AcnB_Swivel; 1.
DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR Gene3D; 1.25.40.310; Aconitate B, HEAT-like domain; 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 NCBIfam; TIGR00117; acnB; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF4; ACONITATE HYDRATASE B; 1.
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; SSF74778; Aconitase B, N-terminal domain; 1.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR036687-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR036687-1};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR036687-
KW 1}; Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR036687};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036687-1};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|PIRNR:PIRNR036687}.
FT DOMAIN 2..130
FT /note="Aconitase B HEAT-like"
FT /evidence="ECO:0000259|Pfam:PF11791"
FT DOMAIN 142..356
FT /note="Aconitase B swivel"
FT /evidence="ECO:0000259|Pfam:PF06434"
FT DOMAIN 446..792
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 218..220
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 388..390
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 684
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT BINDING 743
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT BINDING 746
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT BINDING 765
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT BINDING 770
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
SQ SEQUENCE 839 AA; 90487 MW; 590D8DCFD80D7EE8 CRC64;
MAALVELLKA PPAGEEEFLL DLLINRVPPG VDEAAYVKAG FLAAVAKGEA TSPLVTPEKA
VELLGTMQGG YNIHALIEAL DDEKLAPIAA EALSHTLLMF DNFYDVEEKS KAGNPHAKKI
IQSWADAEWF LKRPKLAEKI TVTVFKVTGE TNTDDLSPAP DAWSRPDIPL HALAMLKNAR
EGIEPDDAGN VGPIKQIEAL QQKGFPLTYV GDVVGTGSSR KSATNSVLWF MGDDIPYVPN
KKGGGVCLGG KIAPIFFNTM EDAGALPIEV DVDRLNMGDV IDIYPYKGEV RNHETGEVLA
NFELKTNVLL DEVRAGGRIP LIIGRGLTTK ARESLGLPHS DVFEQAKDVA ASTRGFSLAQ
KMVGRACGVD GVRPGAYCEP KMTSVGSQDT TGPMTRDELK DLACLGFSAD LVMQSFCHTA
AYPKPVDVTT HHTLPDFIMN RGGVSLRPGD GIIHSWLNRM LLPDTVGTGG DSHTRFPIGI
SFPAGSGLVA FAAATGVMPL DMPESVLVRF KGKMQPGITL RDLVHAIPLY AIKAGLLTVE
KKGKKNIFSG RILEIEGLPD LKVEQAFELS DASAERSAAG CSIKLGKDPI IEYLNSNIVL
LKWMISEGYG DRRTIERRIQ GMEKWLADPQ LMEGDADAEY AAVIEIDLAD IKEPILCAPN
DPDDARLLSD VQGTKIDEVF IGSCMTNIGH FRAAGKLLDA HKGQLPTRLW VAPPTKMDAA
QLTEEGYYSV FGKSGARIEI PGCSLCMGNQ ARVADGATVV STSTRNFPNR LGTGANVFLA
SAELSAVASL LGKLPTPEEY LKFMDQVDKT AVDTYRYLNF DQLSQYTDKA DGVIFQTAV
//
