ID A0LK37_SYNFM Unreviewed; 645 AA.
AC A0LK37;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Aconitase {ECO:0000313|EMBL:ABK17789.1};
DE EC=4.2.1.3 {ECO:0000313|EMBL:ABK17789.1};
GN OrderedLocusNames=Sfum_2106 {ECO:0000313|EMBL:ABK17789.1};
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK17789.1, ECO:0000313|Proteomes:UP000001784};
RN [1] {ECO:0000313|EMBL:ABK17789.1, ECO:0000313|Proteomes:UP000001784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000478; ABK17789.1; -; Genomic_DNA.
DR RefSeq; WP_011698958.1; NC_008554.1.
DR AlphaFoldDB; A0LK37; -.
DR STRING; 335543.Sfum_2106; -.
DR KEGG; sfu:Sfum_2106; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_006714_2_3_7; -.
DR InParanoid; A0LK37; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000001784; Chromosome.
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 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; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR006250; Aconitase_put.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01342; acon_putative; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 1.
DR Pfam; PF00330; Aconitase; 2.
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 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:ABK17789.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001784}.
FT DOMAIN 8..283
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 284..407
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 521..578
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 645 AA; 69661 MW; 33E0526BB20AE60B CRC64;
MAKNLTRKIL EAHLVEGRLT PGEEIAITID HVLLQDATGT MAMLEFEALG LDRIKAQLAV
QYVDHNLLQT DHKNADDHRF LQTASARYGI HFSPAGNGVS HQVHMERFGV PGKTLLGADS
HTPGAAGISM LGIGAGGLDV ALAMAGYPYH LPCPRVLGVK LTGRLPDWVS AKDVILEMLR
RYGVKNCVGK IVEYYGPGVE SLSATDRETI GNMGTELGAT TTLFPSDENT RIYMAAQGRE
SDWVSLHGDE GAEYDEYAEI DLSALEPLIA RPSSPGNVVA VREVAGLKVD QVIVGSSVNS
SFRDLMAVAK TVEGRKAHPR VSFHVNPGSR QVLENVAARG GLIALLKAGA RIHEPGCLGC
IGMGQAPGTG EVSLRTMPRN FPGRSGTKDD QVYLCSPETV AAAALKGVIT DPRDLAAEIA
YPRIRDPEKY LVDASSIIHP SEELSRTEVL RGPNIKPLPE MGPLPETLEA EVILKVGDNI
STDTIMPAGN KVLPLRSNIY AISEFVFSQI DPDFHKECRG KGDLVVVGGE NYGQGSSREH
AALAPRYLGV RVKIAKGFAR IHMSNLCNFG VIPLVFRNPG DYDVLSKGDR VVFREVRRHV
ENGDEEIPLE VNGRSIVTLL KVSARQRRLL LAGGALNFVK QGLLL
//