ID A0A1I6JFJ8_9BURK Unreviewed; 862 AA.
AC A0A1I6JFJ8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=SAMN05428960_1494 {ECO:0000313|EMBL:SFR77758.1};
OS Mitsuaria sp. PDC51.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1881035 {ECO:0000313|EMBL:SFR77758.1, ECO:0000313|Proteomes:UP000199246};
RN [1] {ECO:0000313|EMBL:SFR77758.1, ECO:0000313|Proteomes:UP000199246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PDC51 {ECO:0000313|EMBL:SFR77758.1,
RC ECO:0000313|Proteomes:UP000199246};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOZE01000001; SFR77758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6JFJ8; -.
DR STRING; 1881035.SAMN05428960_1494; -.
DR OrthoDB; 9758061at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000199246; 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; 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:UP000199246};
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 474..700
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 700..817
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT REGION 400..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 862 AA; 92521 MW; 993186DEE7EDEFAE CRC64;
MLQAYRQHEA ERAALGIPPL PLDAKQVAEL IELIKTPPAG EEAFLLDLLT HRVPPGVDDA
AKVKASFLAA VAHGDLKVGL ISKAKATELL GTMVGGYNVH PLIELLDDAE VAGVAADGLK
KTLLMFDYFN DVAAKAKAGN AKAKEVMQSW ADAEWFTSRP EVEKKITVTV FKVPGETNTD
DLSPAPDAWS RPDIPLHYLA MLKNTRPDAA FKPEEDGKRG PMQFIEDLKK KGHVVAYVGD
VVGTGSSRKS ATNSVIWATG QDIPFVPNKR FGGVTLGGKI APIFFNTQED SGSLPIEVDV
SKLEMGDVID VLPYDGKLVK NGETVAEFKL KSDVLFDEVR AGGRINLIIG RSLTAKAREF
LGLPASTLFR LPQAPAASNA GFTLAQKMVG RAVGLPEGQG VRPGTYCEPK MTTVGSQDTT
GPMTRDELKD LACLGFSADL VMQSFCHTAA YPKPVDVKTH RELPAFISNR GGVSLRPGDG
VIHSWLNRLL LPDTVGTGGD SHTRFPIGIS FPAGSGLVAF GAATGVMPLD MPESVLVRFK
GEMQPGVTLR DLVHAIPLYA IKAGLLTVAK AGKKNIFSGR ILEIEGLPDL KVEQAFELSD
ASAERSAAGC TIKLNPAPIK EYLTSNIVLM KNMIADGYAD AKTLQRRIEK VEAWLAKPDL
LEADKDAEYA AVIEIDLADI TEPIVCCPND PDDAKVLSEV AGTKIDEAFI GSCMTNIGHF
RAAAKLLGGQ RDIPVKLWVA PPTKMDQSEL IKEGHYAAFG TAGARTEMPG CSLCMGNQAQ
VREGATVIST STRNFPNRLG KNTNVFLGSA ELAAIASRLG RLPTKAEYLK EMGVIDADKA
SVYRYMNFDQ IEEYAETAKS VA
//
