ACNB_HELPJ
ID ACNB_HELPJ Reviewed; 852 AA.
AC Q9ZL64;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=jhp_0716;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD06299.1; -; Genomic_DNA.
DR PIR; D71896; D71896.
DR RefSeq; WP_010882558.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZL64; -.
DR SMR; Q9ZL64; -.
DR STRING; 85963.jhp_0716; -.
DR PRIDE; Q9ZL64; -.
DR EnsemblBacteria; AAD06299; AAD06299; jhp_0716.
DR KEGG; hpj:jhp_0716; -.
DR PATRIC; fig|85963.30.peg.261; -.
DR eggNOG; COG1049; Bacteria.
DR OMA; QDTTGAM; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
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; RNA-binding;
KW Tricarboxylic acid cycle.
FT CHAIN 1..852
FT /note="Aconitate hydratase B"
FT /id="PRO_0000076677"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 237..239
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 405..407
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 489
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 708
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 766
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 769
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 788
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 793
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 852 AA; 92742 MW; F9623403AF2556A9 CRC64;
MKDFLEDYKK SVLERKSEGI PPLPLNAKQV EAVVEILMKD PTNAAFAKEL LIHRVSPGVD
EGAKVKAEFL AQLSQKKLEC PHISALEATT LLGTMLGGYN VEPLIVGLES QDKNIAKESA
KALKTTLLVY GSFDKIAAMS KTNALAKEVL ESWANAEWFL NKEPLNECIE ACVFKIDGET
NTDDLSPASD AFTRSDIPLH AKAMLKNRIE NYEQRIEAIK TKGVPVAYVG DVVGTGSSRK
SATNSIMWHF GKDIPFVPNK RSGGIVIGGV IAPIFFATCE DSGALPIVAD VKDLKEGDII
KIYPYKGEIT LNDKVVSTFK LEPETLLDEV RASGRIPLII GRGLTNKARK FLGLGESEAF
KKPSAPKSDA KGYTLAQKIV GHACGVKGIL PGAYCEPKVT TVGSQDTTGA MTRDEVKELA
SLKFDAPFVL QSFCHTAAYP KPSDVSLHAT LPGFITQRGG VALHPGDGVI HTWLNRMGLP
DTLGTGGDSH TRFPLGISFP AGSGLVAFAA VTGTMPLNMP ESVLVRFKGE MNPGITLRDL
VNAIPYYAIK KGLLTVEKKG KINVFNGRIL EIEGLPDIKM EQAFELSDAS AERSAAACVV
RLNKEPMIEY LKSNIKLIDE MIASGYEDKE TLKKRRDAMQ AWVDKPVLLE PDSNAQYAAV
IEIDVAEITE PILACPNDPD DVATLSEVLA DTTGKRPHAI DEVFIGSCMT NIGHFRAFGE
IVKNAPPSQA RLWVVPPSKM DEQELINEGY YAIFGAAGAR TEVPGCSLCM GNQARVRDNA
VVFSTSTRNF DNRMGRGAKV YLGSAELGAA CALLGRIPTK EEYMNLVSEK LESQKDKIYR
YMNFNLMENF RL
