ID E3BNP9_9VIBR Unreviewed; 861 AA.
AC E3BNP9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN ORFNames=VIBC2010_14699 {ECO:0000313|EMBL:EFP95293.1};
OS Vibrio caribbeanicus ATCC BAA-2122.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=796620 {ECO:0000313|EMBL:EFP95293.1, ECO:0000313|Proteomes:UP000002943};
RN [1] {ECO:0000313|EMBL:EFP95293.1, ECO:0000313|Proteomes:UP000002943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2122 {ECO:0000313|EMBL:EFP95293.1,
RC ECO:0000313|Proteomes:UP000002943};
RX PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT Scleritoderma cyanea.";
RL Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:EFP95293.1}.
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DR EMBL; AEIU01000096; EFP95293.1; -; Genomic_DNA.
DR AlphaFoldDB; E3BNP9; -.
DR STRING; 796620.VIBC2010_14699; -.
DR eggNOG; COG1048; Bacteria.
DR Proteomes; UP000002943; Unassembled WGS sequence.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
DR Gene3D; 6.10.190.10; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR012708; 2Me_IsoCit_deHydtase_FeS-dep.
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; IPR006249; Aconitase/IRP2.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR02333; 2met_isocit_dHY; 1.
DR PANTHER; PTHR11670:SF43; 2-METHYLCITRATE DEHYDRATASE (2-METHYL-TRANS-ACONITATE FORMING); 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:EFP95293.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002943}.
FT DOMAIN 67..535
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 658..788
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 861 AA; 95020 MW; 8CE47AE41EABAEB7 CRC64;
MNSSYRKPLP GTQLDFFDVR EAVNTVSSGS YDKLPYTSRV LAEQIVRRCD SDILIQSLEQ
IIYRKRDHDF PWYPARVVCH DILGQTALVD LAGLRDAINQ QGGDPSKVNP VVETQLIVDH
SLAVEHAGFE SDAFEKNRAI EDRRNEDRFH FIDWCKTAFE NVSVIPAGNG IMHQINLEKM
SPVVQSQHGV AFPDTCVGTD SHTPHVDALG VIAIGVGGLE AETVMLGRPS MMRLPDIVGV
HLTGERQPGI TATDIVLALT EFLRQKRVVS SYLEFFGEGT KGLTIGDRAT ISNMTPEYGA
TAAMFYIDQQ TIDYLKLTGR DDKQVALVEN YAKTVGLWSE QLLTAQYERV LEFNLSNVCR
NLAGPSNPHR RLPTSELMTQ GVATSQQIQP SNGTLPDGAV IIAAITSCTN TSNPRNVVAA
GLVAKKANAL GLTRKPWVKS SFAPGSKVAK LYLEESGLLK ELEALGFGIV AYACTTCNGM
SGALDPEIQK EIIDQDVYTT AVLSGNRNFD GRIHPYAKQA FLASPPLVVA YALAGSIRFD
IESGVLGEDI NGVPIFLSDL WPTDEEIDAI VNKHVRPDQF NQVYIEMFKL EEENTPKFPL
YEWRPQSTYI RRPPYWEGAL AGERQLKNMR PLAILGDNIT TDHLSPSNAI LASSAAGEYL
TFMGVPEEDF NSYATHRGDH LTAQRATLAN PKLFNEMVRD NGNIIQGSLA RIEPEGKVTR
MWEAIECYME RKQPLLIIAG ADYGQGSSRD WAAKGVRLAG VQVIVAEGFE RIHRTNLIGM
GVLPLEFRLG TDRKTLQLDG SETYDVIGDI YPGSSLTLRV SRKNGACENV DLLCRLDTED
EVNVYQAGGV LQRFAKDFLS Q
//
