ID   Q0K3Q9_CUPNH            Unreviewed;       863 AA.
AC   Q0K3Q9;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 126.
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   Name=acnB {ECO:0000313|EMBL:CAJ95365.1};
GN   OrderedLocusNames=H16_B0568 {ECO:0000313|EMBL:CAJ95365.1};
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ95365.1, ECO:0000313|Proteomes:UP000008210};
RN   [1] {ECO:0000313|EMBL:CAJ95365.1, ECO:0000313|Proteomes:UP000008210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC   337 {ECO:0000313|Proteomes:UP000008210};
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Potter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
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}.
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DR   EMBL; AM260480; CAJ95365.1; -; Genomic_DNA.
DR   RefSeq; WP_010810392.1; NZ_CP039288.1.
DR   AlphaFoldDB; Q0K3Q9; -.
DR   STRING; 381666.H16_B0568; -.
DR   GeneID; 57646456; -.
DR   KEGG; reh:H16_B0568; -.
DR   eggNOG; COG1049; Bacteria.
DR   HOGENOM; CLU_016536_0_0_4; -.
DR   OrthoDB; 9758061at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000008210; Chromosome 2.
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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000008210};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|PIRNR:PIRNR036687}.
FT   DOMAIN          4..156
FT                   /note="Aconitase B HEAT-like"
FT                   /evidence="ECO:0000259|Pfam:PF11791"
FT   DOMAIN          168..382
FT                   /note="Aconitase B swivel"
FT                   /evidence="ECO:0000259|Pfam:PF06434"
FT   DOMAIN          473..700
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          699..816
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT   BINDING         246..248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT   BINDING         417..419
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT   BINDING         501
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT   BINDING         713
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT   BINDING         771
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT   BINDING         774
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-1"
FT   BINDING         793
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
FT   BINDING         798
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036687-2"
SQ   SEQUENCE   863 AA;  93126 MW;  6624228948299E1E CRC64;
     MLENYRAHVA ERAALGIPPL PLTAKQTAEL VELLKNPPAG EEQTLVELIT YRVPAGVDDA
     AKVKASYLAA VALGKEKCAL ISRAKATELL GTMLGGYNIS PLIELLDDAE VGTVAAEALK
     KTLLMFDAFH DVKEKADQGN ANAKAVLQSW ADAEWFTSRP EVPQSLTITV FKVPGETNTD
     DLSPAPDATT RPDIPMHALA MLKNKREGAA FQPEEDGKRG PVKFIESLKE KGHLVAYVGD
     VVGTGSSRKS ATNSVLWFTG EDIPFIPNKR FGGVCLGNKI APIFYNTMED AGALPIELDV
     SKMEMGDVVE LRPYEGKALK DGAVIAEFKV KSDVLFDEVR AGGRIPLIVG RGLTAKAREA
     LGLAPSTLFR LPQNPADTGR GFTLAQKMVG RACGLPEGKG IRPGTYCEPK MTSVGSQDTT
     GPMTRDELKD LACLGFSADL VMQSFCHTAA YPKPVDVKTH HTLPEFISTR GGISLRPGDG
     VIHSWLNRML LPDTVGTGGD SHTRFPIGIS FPAGSGLVAF AAATGVMPLD MPESVLVRFK
     GKMQPGVTLR DLVNAIPLYA IKQGLLTVAK QGKKNIFSGR VLEIEGLPDL KVEQAFELSD
     ASAERSAAGC TVRLNKDPII EYINSNITLL KWMIAQGYQD PRSLQRRIKA MEAWLADPKL
     LEPDADAEYA AVIEIDLADV HEPIVACPND PDDVKTLSEV AGAKIDEVFI GSCMTNIGHF
     RAASKLLEGK RDIPVKLWVA PPTKMDQKQL TEEGHYGVFG TAGARTEMPG CSLCMGNQAQ
     VREGATVMST STRNFPNRLG KNTNVYLGSA ELAAICSRLG RIPTKEEYMA DMGVLNANGD
     KIYKYMNFDQ IEDFKEVADG VTV
//