ID L9VN17_9EURY Unreviewed; 908 AA.
AC L9VN17;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN ORFNames=C496_17552 {ECO:0000313|EMBL:ELY38451.1};
OS Natronorubrum tibetense GA33.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=1114856 {ECO:0000313|EMBL:ELY38451.1, ECO:0000313|Proteomes:UP000011599};
RN [1] {ECO:0000313|EMBL:ELY38451.1, ECO:0000313|Proteomes:UP000011599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GA33 {ECO:0000313|EMBL:ELY38451.1,
RC ECO:0000313|Proteomes:UP000011599};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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 -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELY38451.1}.
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DR EMBL; AOHW01000042; ELY38451.1; -; Genomic_DNA.
DR RefSeq; WP_006091562.1; NZ_KB913017.1.
DR AlphaFoldDB; L9VN17; -.
DR STRING; 1114856.GCA_000383975_00185; -.
DR PATRIC; fig|1114856.3.peg.3638; -.
DR eggNOG; arCOG01697; Archaea.
DR OrthoDB; 255at2157; -.
DR Proteomes; UP000011599; Unassembled WGS sequence.
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 CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 6.10.190.10; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR044137; AcnA_IRP_Swivel.
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; IPR006249; Aconitase/IRP2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01341; aconitase_1; 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR PANTHER; PTHR11670:SF54; CYTOPLASMIC ACONITATE HYDRATASE; 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.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:ELY38451.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 77..576
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 707..833
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 908 AA; 99425 MW; 163DAC8A6CA978F7 CRC64;
MAIDEFSDAI REFEHDGETY KMADLTVLEE QGLCDLEKLP VSIRVLLEAV LRNADGDMIS
AQDVENAASW QPEVPDVEVP FQPSRVVLQD LTGVPAVVDL AALRSAADRA DKDPSIVEPE
VPCDLVIDHS VQVDYFGSED AYEQNVELEY ERNEERYRAI KWAEQAFEDF NVVPPGTGIV
HQVNLEHLGE VVHAREEDGE QWLLPDTLVG TDSHTPMING IGVVGWGVGG IEAEAALLGQ
PITMTLPEVV GVELTGELPE GATATDLVLH ITEKLRQVGV VDKFVEFYGD GVSQLSVADR
ATISNMSPEH GCTISMFPVD EKTLDYLELT GRDEDHIELV REYLEAQGLF GDHDPEFTET
VEFDLGSVEP SLAGHKKPHA RIPMGDLDEH FPTLLEEQGV IPSGAAESDG GLVAKEQPGL
DEKIPVTLED GTEVEIGHGS VLVSAITSCT NTSNPSVMVA AGLLARNALE QGLDVPDYVK
TSLAPGSKVV TEYLKQADLL EDLEGLGYHV VGYGCTTCIG NAGPLAEPIE AAIDEHDLWT
TSVLSGNRNF EARIHPKIRA NYLASPPLVV AYGLAGKMDI DLETEPIGTN DDGEEIFLED
IWPDPEEVRQ TIHESVSAEL FKDKYASVFE GDDRWEALDA PTGDVYEWDS ESTYIREPPF
FQDFPLEEPG VEDIADARCL LTLGDTVTTD HISPAGPFSE DLPAGQWLSE RGVEPYEFNT
YGSRRGNHEV MMRGTFANVR IENQLLDGKE GGYTIHHPTE EETTVFEASE RYRDEDTPLI
VMAGEELGTG SSRDWAAKGT DLLGIRATIG QSYERIYRDN LLGMGVLPLQ FEDGEGWEEL
GLDGSEYFDI KGLDDGLEPN AELTVVAEDD DGETTEFDVT AQVGTPAAVK YVENGGVLHL
VLRRMLTE
//