ACNB_HELPY
ID ACNB_HELPY Reviewed; 852 AA.
AC P56418;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 136.
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=HP_0779;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD07828.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; AE000511; AAD07828.1; ALT_INIT; Genomic_DNA.
DR PIR; C64617; C64617.
DR RefSeq; NP_207572.1; NC_000915.1.
DR RefSeq; WP_001863439.1; NC_000915.1.
DR AlphaFoldDB; P56418; -.
DR SMR; P56418; -.
DR DIP; DIP-3210N; -.
DR IntAct; P56418; 5.
DR MINT; P56418; -.
DR STRING; 85962.C694_04000; -.
DR PaxDb; P56418; -.
DR PRIDE; P56418; -.
DR EnsemblBacteria; AAD07828; AAD07828; HP_0779.
DR KEGG; hpy:HP_0779; -.
DR PATRIC; fig|85962.47.peg.831; -.
DR eggNOG; COG1049; Bacteria.
DR OMA; QDTTGAM; -.
DR PhylomeDB; P56418; -.
DR BioCyc; MetaCyc:HP0779-MON; -.
DR SABIO-RK; P56418; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000000429; 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..852
FT /note="Aconitate hydratase B"
FT /id="PRO_0000076676"
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; 92663 MW; 7051382D8A0D0AB3 CRC64;
MKDFLEDYKK SVSERGSEGI PPLPLNAKQV QAVVEILTKD PTNAAFAKEL LIHRVSPGVD
EGAKVKAEFL AKLSQKKLEC VHISALEATT LLGTMLGGYN VEPLIMGLES QDKNIAKESA
KALKTTLLVY GSFDKIAAMS KTNALAKEVL ESWANAEWFL NKEPLNECIE ACVFKIDGET
NTDDLSPASD AFTRSDIPLH AKAMLKNRIE NYEQRIKAIK TKGVPVAYVG DVVGTGSSRK
SATNSIMWHF GKDIPFVPNK RSGGIVIGGV IAPIFFATCE DSGALPIVAD VKDLKEGDLI
KIYPYKGEIT LNDKVVSTFK LEPETLLDEV RASGRIPLII GRGLTNKARK FLGLGESEAF
KKPSAPKSDA KGYTLAQKIV GHACGVKGIL PGTYCEPKVT TVGSQDTTGA MTRDEVKELA
SLKFDAPFVL QSFCHTAAYP KPSDVSLHAT LPGFITQRGG VALHPGDGVI HTWLNRMGLP
DTLGTGGDSH TRFPLGISFP AGSGLVAFAA VTGTMPLNMP ESVLVRFKGE MNPGITLRDL
VNAIPYYAIK KGLLTVEKKG KINVFNGRIL EIEGLPDIKM EQAFELSDAS AERSAAACVV
RLNKEPMIEY LKSNIKLIDE MIASGYEDKE TLKKRRDAMQ AWVDNPVLLE PDSNAQYAAV
IEIDVAEITE PILACPNDPD DVATLSEVLA DTTGKRPHAI DEVFIGSCMT NIGHFRAFGE
IVKNAPPSQA RLWVVPPSKM DEQELINEGY YAIFGAAGAR TEVPGCSLCM GNQARVRDNA
VVFSTSTRNF DNRMGRGAKV YLGSAELGAA CALLGRIPTK EEYMNLVSEK LESQKDKIYR
YMNFNLMENF RL
