ID A0A2N7QMN6_9GAMM Unreviewed; 863 AA.
AC A0A2N7QMN6;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:PMQ02901.1};
GN ORFNames=DyAD56_21760 {ECO:0000313|EMBL:PMQ02901.1};
OS Dyella sp. AD56.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1528744 {ECO:0000313|EMBL:PMQ02901.1, ECO:0000313|Proteomes:UP000235676};
RN [1] {ECO:0000313|EMBL:PMQ02901.1, ECO:0000313|Proteomes:UP000235676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD56 {ECO:0000313|EMBL:PMQ02901.1,
RC ECO:0000313|Proteomes:UP000235676};
RA Schulz-Bohm K., Janssens T.K., De Jager V., Gawehns F., De Boer W.,
RA Garbeva P.;
RT "Bacterial performance in fungal presence.";
RL Submitted (AUG-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PMQ02901.1}.
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; NRDP01000035; PMQ02901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7QMN6; -.
DR OrthoDB; 9758061at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000235676; 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; 1.
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.
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:UP000235676};
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..816
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT REGION 401..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 863 AA; 92904 MW; C6BC12C11C87751C CRC64;
MLNAYRQHVA ERAALGIPPL PLSAQQTADL IELLKNPPAG EEAFLVDLIT NRVPAGVDDA
AKVKASYLAA VAFGTEKSAL ISREKATELL GTMLGGYNIH PLIELLDDAQ IGTVAANALK
HTLLMFDAFH DVKEKADKGN ANAKAVLQSW ADAEWFTSKP EVPESLTITV FKVPGETNTD
DLSPAPDATT RPDIPLHALA MLKNKRDGAP FQPEEDGKRG PIAFIESLKE KGHLVAYVGD
VVGTGSSRKS ATNSVLWFTG ENIPFIPNKR FGGVCLGSKI APIFYNTMED AGALPIELDV
SSMEMGDVVE LRPYDGKALK NGEVIAEFQV KSDVLFDEVR AGGRIPLIIG RGLTAKAREA
LGLPVSTLFR LPQQPVDTGK GFTLAQKMVG RAIGLPEGQG VRPGTYCEPK MTSVGSQDTT
GPMTRDELKD LACLGFSADL VMQSFCHTAA YPKPVDVKTH HTLPEFISTR GGISLRPGDG
VIHSWLNRML LPDTVGTGGD SHTRFPIGIS FPAGSGLVAF AAATGVMPLD MPESVLVRFK
GELQPGVTLR DLVNAIPLYA IKQGLLTVAK QGKKNIFSGR ILEIEGLPNL KVEQAFELSD
ASAERSAAGC TVHLDKAPII EYITSNITLL KYMIAQGYKD PRSLQRRIKA MEAWLANPQL
LDRDADAEYA AVIEIDLADV HEPIVACPND PDDVKTLSDV AGATIDEVFI GSCMTNIGHF
RAASKLLEGK RDIPTKLWVA PPTKMDQQQL TEEGHYGVLG TAGARMEMPG CSLCMGNQAQ
VREGATVFST STRNFPNRLG KNSNVYLGSA ELAAICSRLG KIPTKEEYMT DVGVINANGD
KIYKYMNFDQ IKDYSEVAAA VPV
//