ID E1QJ13_DESB2 Unreviewed; 639 AA.
AC E1QJ13;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Aconitate hydratase {ECO:0000313|EMBL:ADK85556.1};
GN OrderedLocusNames=Deba_2192 {ECO:0000313|EMBL:ADK85556.1};
OS Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS / 2st14).
OC Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC Desulfarculaceae; Desulfarculus.
OX NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK85556.1, ECO:0000313|Proteomes:UP000009047};
RN [1] {ECO:0000313|EMBL:ADK85556.1, ECO:0000313|Proteomes:UP000009047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC {ECO:0000313|Proteomes:UP000009047};
RX PubMed=21304732; DOI=10.4056/sigs.1243258;
RA Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL Stand. Genomic Sci. 3:276-284(2010).
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DR EMBL; CP002085; ADK85556.1; -; Genomic_DNA.
DR RefSeq; WP_013258997.1; NC_014365.1.
DR AlphaFoldDB; E1QJ13; -.
DR STRING; 644282.Deba_2192; -.
DR KEGG; dbr:Deba_2192; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_006714_2_3_7; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000009047; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009047}.
FT DOMAIN 8..285
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 283..407
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 517..574
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 639 AA; 67150 MW; 9087263AC376090F CRC64;
MAKTLARKII EEHLVEGRCQ PGEEIGLRID QTLTQDATGT LAALEFEALG LERVRTEVSV
SYVDHNILQS DFKNPDDHRF LRSIAARYGL WFSPPGNGIC HQLHMLNFGR PGATLLGSDS
HTPHGGGLGM LAMGAGGLDV AAAMAGQPFF LTYPKVLGVR LSGKLSPWVG AKDVILELLR
RLSVKGGLGY VVEYHGPGVT GLSVLQRAAI TNMGAELGAT SSVFPSDEKT KAFLTAQGRA
DAWREMSADD GAVYDKLEEI DLAALEPLAA CPSSPDAVRP VRELAEVAVE QVIVGSCGGG
SYEDLMTIAM ALKGKALAPG LNLSVNPGSR QALAQVTANG ALLDMLEAGV RLHQAGCLGC
IGMSQAPATG AASVRTFPRN FPGRSGTKDD RVYLTGPEVA AATALAGHLA DPRQVFGPQE
PIPPAPAVRP EALVAPPADG AGVAIVRGPN IAPFPQLPPL ADDLVCTVAL KVGDNITTDH
IMPAGSKILP LRSNVPAISQ FVFNAVDPDF PAKAQACAPA AVVGGDNYGQ GSSREHAALA
PRYLGVQVKL AKSFARIHKA NLINFGVLPL VFADPADYDR LDEGQRIELR GVKRALLEGA
ENLTALVDGQ PVELRLEASP RDRQILAAGG RLNHIKNAL
//
