ID C6WZV2_FLAB3 Unreviewed; 768 AA.
AC C6WZV2;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE AltName: Full=Citrate hydro-lyase {ECO:0000256|ARBA:ARBA00029682};
DE AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN OrderedLocusNames=FIC_00162 {ECO:0000313|EMBL:ACU06637.1};
OS Flavobacteriaceae bacterium (strain 3519-10).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=531844 {ECO:0000313|EMBL:ACU06637.1, ECO:0000313|Proteomes:UP000001512};
RN [1] {ECO:0000313|EMBL:ACU06637.1, ECO:0000313|Proteomes:UP000001512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3519-10 {ECO:0000313|EMBL:ACU06637.1,
RC ECO:0000313|Proteomes:UP000001512};
RX PubMed=18622572; DOI=10.1007/s00792-008-0178-2;
RA Raymond J.A., Christner B.C., Schuster S.C.;
RT "A bacterial ice-binding protein from the Vostok ice core.";
RL Extremophiles 12:713-717(2008).
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 -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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; CP001673; ACU06637.1; -; Genomic_DNA.
DR AlphaFoldDB; C6WZV2; -.
DR STRING; 531844.FIC_00162; -.
DR KEGG; fba:FIC_00162; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_006714_2_2_10; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000001512; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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:UniProtKB-UniPathway.
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 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; IPR015932; Aconitase_dom2.
DR InterPro; IPR006248; Aconitase_mito-like.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01340; aconitase_mito; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 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.
DR PROSITE; PS00450; ACONITASE_1; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:ACU06637.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001512}.
FT DOMAIN 45..488
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 569..696
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 768 AA; 83168 MW; B116DD023AC3F64F CRC64;
MVFLNLNTSN MIFDFDMIQA VYARYPERIA KARETVGKPL TLSEKILYTH LWAGNATEAH
ERGNSYVDFA PDRVAMQDAT AQMALLQFMQ AGKPQVAVPS TAHADHLIQA RVGAEADLQE
GINKNSEVFN FLSSVCDKYG IGFWKPGAGI IHQVVLENYA FPGGMMIGTD SHTVNAGGLG
MVAIGVGGAD AVDVMAGMAW ELKMPKLIGV KLTGRLNGWT SAKDIILKVA GILTVKGGTG
CIIEYFGDGA ESLSATGKGT ICNMGAEVGA TTSTFGYDDS MRRYLAATGR QAVVDEADKI
AEHLTGDAEV YANPELYFDQ VIEINLDELA PHLNGPFTPD LATPVSEFRA KAEANGWPLD
VEWALIGSCT NSSYEDLSRA ASIVEDAVAK GVKPKAILGI NPGSEQVKFT AERDGFLDSF
RKFESARIFT NACGPCIGQW DREGADKGEK NSIIHSFNRN FAKRADGNPN THAFVASPEM
VAAIAISGRL DFNPITDTLL NQNGEQIRLN EPNGFELPAK GFAVDDNGYQ APSADGTQVR
VDVSPTSDRL QLLEPFEPWN GKNITGAKLL IKAFGKCTTD HISMAGPWLK YRGHLDNISN
NMLIGAINAY NMETNKVKNG LSGDYDEVPN VARAYKAAGI PTIVVGDHNY GEGSSREHAA
MEPRHLGVRA VLVKSFARIH ETNLKKQGML GLTFANADDY DKIFEDDTIN FLDLEQFAPG
RPLQLEFLHA DGTKDVIVAN HTYNAQQVGW FRAGSALNLI AEEAKRTA
//
