ACNB_SYNY3
ID ACNB_SYNY3 Reviewed; 868 AA.
AC P74582;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
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=slr0665;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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; BA000022; BAA18689.1; -; Genomic_DNA.
DR PIR; S76777; S76777.
DR AlphaFoldDB; P74582; -.
DR SMR; P74582; -.
DR IntAct; P74582; 4.
DR STRING; 1148.1653778; -.
DR PaxDb; P74582; -.
DR PRIDE; P74582; -.
DR EnsemblBacteria; BAA18689; BAA18689; BAA18689.
DR KEGG; syn:slr0665; -.
DR eggNOG; COG1049; Bacteria.
DR InParanoid; P74582; -.
DR OMA; QDTTGAM; -.
DR PhylomeDB; P74582; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000001425; 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.
DR PROSITE; PS01244; ACONITASE_2; 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..868
FT /note="Aconitate hydratase B"
FT /id="PRO_0000076678"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 235..237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 404..406
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 488
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 700
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 758
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 761
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 780
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 785
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 868 AA; 93552 MW; EBF93B0F966A94EE CRC64;
MLQAYRRHVA DRQKLGIPPL PLNAQQTTEL CELLKNPPEA EKEELMMLLR DRVPPGVDEA
AYVKAGFLTA IAKGEVTCPL ISGQGAVDLL GTMIGGYNVQ SLIELLKSKD TNIASAAATA
LSKTLLVFDA FNDVLHLSDT NGYAKQVIDA WAEGAWFINK PEVPERITVT VFKVPGETNT
DDLSPAPHAT TRPDIPLHAL AMLEAKMPEG LGTIAELKQK GHPVAYVGDV VGTGSSRKSA
INSVLWHIGT DIPFVPNKRA GGYILGGKIA PIFFNTAEDS GALPIECDVN QLNTGDVITI
YPREGKITNK AGETITTFQL KPETILDEVR AGGRIPLLIG RALTDKTREA LGLSPSPLFV
RPTAPADTGK GFTLAQKMVG KACGVQGIRP GTSCEPIMTT VGSQDTTGPM TRDELKELAC
LGFNADLTLQ TFCHTAAYPK PVDIKTHKDL PDFFSTRGGV ALRPGDGIIH SWLNRMLLPD
TVGTGGDSHT RFPLGISFPA GSGLVAFAAA LGVMPLDMPE SVLVKFTGEL QPGVTLRDIV
NAIPWVAMQQ GKLTVGKGDK VNVFNGRIME MEGLPDLKVE QAFELTDATA ERSCSGSTIK
LSEETVAEYL RSNVVLMKNM IARGYQDART LLRRIAKMEE WLANPSLMSG DADAEYADVI
EVNLDEIKEP IVAAPNDPDN VKLMSECAGD VIHEVFIGSC MTNIGHYRAA AKILEGAGTV
KGRLWICPPT RMDEQQLREE GIYGIFAAAG ARTEMPGCSL CMGNQARVED GVTVFSTSTR
NFNNRMGKGA QVYLGSAELA AVCALLGKIP TVEEYLAIVS EKVAPFEGEL YRYLNFNEID
NFEDFGRVIP LDQMPKIEDI LGMPVGAK
