ID M1Y5N1_NATM8 Unreviewed; 661 AA.
AC M1Y5N1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Aconitate hydratase {ECO:0000313|EMBL:CCQ37880.1};
DE EC=4.2.1.3 {ECO:0000313|EMBL:CCQ37880.1};
GN Name=citB {ECO:0000313|EMBL:CCQ37880.1};
GN OrderedLocusNames=Nmlp_3767 {ECO:0000313|EMBL:CCQ37880.1};
OS Natronomonas moolapensis (strain DSM 18674 / CECT 7526 / JCM 14361 /
OS 8.8.11).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=268739 {ECO:0000313|EMBL:CCQ37880.1, ECO:0000313|Proteomes:UP000011867};
RN [1] {ECO:0000313|EMBL:CCQ37880.1, ECO:0000313|Proteomes:UP000011867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18674 / JCM 14361 / 8.8.11
RC {ECO:0000313|Proteomes:UP000011867};
RX PubMed=23516216; DOI=10.1128/genomeA.00095-13;
RA Dyall-Smith M.L., Pfeiffer F., Oberwinkler T., Klee K., Rampp M., Palm P.,
RA Gross K., Schuster S.C., Oesterhelt D.;
RT "Genome of the haloarchaeon Natronomonas moolapensis, a neutrophilic member
RT of a previously haloalkaliphilic genus.";
RL Genome Announc. 1:e0009513-e0009513(2013).
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DR EMBL; HF582854; CCQ37880.1; -; Genomic_DNA.
DR RefSeq; WP_015410607.1; NC_020388.1.
DR AlphaFoldDB; M1Y5N1; -.
DR STRING; 268739.Nmlp_3767; -.
DR GeneID; 14652785; -.
DR KEGG; nmo:Nmlp_3767; -.
DR eggNOG; arCOG01697; Archaea.
DR HOGENOM; CLU_006714_2_3_2; -.
DR OMA; GCIGMGQ; -.
DR OrthoDB; 255at2157; -.
DR Proteomes; UP000011867; 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; IPR018136; Aconitase_4Fe-4S_BS.
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:SF4; ACONITATE HYDRATASE B; 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 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:CCQ37880.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011867}.
FT DOMAIN 7..407
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 532..583
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 638..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 71143 MW; F1EEEACECC09F044 CRC64;
MGQTLTEKIL DDHLVEGDLE TGEEIGIEID QVLTQDTTGT LVWLQFEALG LDEVQTELAA
QYCDHQTYQF DFKNTDDHRF LRSAAGTFGA YYSRPGNGIC HNVHKENFAA PGKTLLGSDS
HTPTPGGLGQ LAIGSGGLDV SVAMGGGAYY IEMPEVVNVH LEGELPEWAT AKDIALHLLG
ELTVKGGVGK IFEYTGPGVE SLTVPERTTI TNLGTELGAT SSIFPTDEKT KDWLSRIGRE
DDYVDLSPDE DAEYADQITV DLSELEPLIA CPSMPDKVVP VSEVAGEDVE QVIIGSCTNG
AYEDILPGAK MLKGRTVEKK TEMVVAPGSK QASEMLAREG WTAEMMAAGV NFSEATCGAC
IGIGHVPGSD SVSLRTFNRN FEGRSGIEDD NVYLCSPEVA TAAAIAGEIV DPRDLADDLG
DLEAPEFEMG SKYSEGMGQE DPDIIAPDEA VDDELIKGPN IGDVPLKDEM GSELSGPNLL
KMEDNITTDH IIPATQDILM YRSNIPKLSE FTLSRVDEDF AQRALDSDGG FLVAGENYGQ
GSSREHAALC PMYLGVEGVL AQSFARIHKA NLFNFGLIPL EIDASDYEQI EQGDDIEIVD
DVADAVRSGQ EEFTVRVNDE WELTATLDAS ERERRILADG GKLSHTKKQA EGGSDAAPAD
D
//