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Database: UniProt
Entry: A0LK37_SYNFM
LinkDB: A0LK37_SYNFM
Original site: A0LK37_SYNFM 
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
//
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