ID A0A231MTN0_9GAMM Unreviewed; 485 AA.
AC A0A231MTN0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase {ECO:0000313|EMBL:OXS13544.1};
DE Flags: Fragment;
GN ORFNames=CGX12_19200 {ECO:0000313|EMBL:OXS13544.1};
OS Zobellella denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Zobellella.
OX NCBI_TaxID=347534 {ECO:0000313|EMBL:OXS13544.1, ECO:0000313|Proteomes:UP000215233};
RN [1] {ECO:0000313|EMBL:OXS13544.1, ECO:0000313|Proteomes:UP000215233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZD1 {ECO:0000313|EMBL:OXS13544.1,
RC ECO:0000313|Proteomes:UP000215233};
RA Wu Y.-W., Chu K.-H.;
RT "Draft genome of Zobellella denitrificans ZD1.";
RL Submitted (JUL-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 -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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:OXS13544.1}.
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DR EMBL; NMUO01000181; OXS13544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A231MTN0; -.
DR OrthoDB; 9758061at2; -.
DR Proteomes; UP000215233; Unassembled WGS sequence.
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:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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; 1.
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; IPR036008; Aconitase_4Fe-4S_dom.
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 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 SUPFAM; SSF74778; Aconitase B, N-terminal domain; 1.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 1..39
FT /note="Aconitase B HEAT-like"
FT /evidence="ECO:0000259|Pfam:PF11791"
FT DOMAIN 51..265
FT /note="Aconitase B swivel"
FT /evidence="ECO:0000259|Pfam:PF06434"
FT DOMAIN 355..482
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OXS13544.1"
FT NON_TER 485
FT /evidence="ECO:0000313|EMBL:OXS13544.1"
SQ SEQUENCE 485 AA; 51846 MW; 92C7235F9D18B0B6 CRC64;
ALSHTLLMFD AFHDVADKAK AGNVHAQQVL QSWADAEWFL GRPALADKIT LTVFKVPGET
NTDDLSPAQD AWSRPDIPLH ALAMLKNARP GIAPDEDGVV GPITAINALK EKGFPLAYVG
DVVGTGSSRK SATNSVLWHM GDDIPFVPNK RAGGVCIGGK IAPIFFNTME DAGALPIECD
VTKLNTGDVI DIYPYEGKVC RHGSDEVLAE FKLKTEVLLD EVRAGGRIPL IIGRGLTDKA
RAELGLGHSE VFKRPADVAD SGKGYTLAQK MVGKACGVAG VRPGQYCEPK MTTVGSQDTT
GPMTRDELKD LACLGFSADL TMQSFCHTAA YPKPVDVVTH HTLPDFIMNR GGVSLRPGDG
VIHSWLNRML LPDTVGTGGD SHTRFPIGIS FPAGSGLVAF AAATGVMPLD MPESVLVRFK
GEMQPGITLR DLVHAIPYYG IKQGLLTVAK EGKINEFSGR VLEIEGLPQL KVEQAFELAD
ATAER
//