ID A0A2G8KKL3_STIJA Unreviewed; 724 AA.
AC A0A2G8KKL3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN ORFNames=BSL78_14647 {ECO:0000313|EMBL:PIK48498.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK48498.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK48498.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK48498.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK48498.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU361275}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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:PIK48498.1}.
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DR EMBL; MRZV01000519; PIK48498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8KKL3; -.
DR STRING; 307972.A0A2G8KKL3; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
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 4Fe-4S {ECO:0000256|RuleBase:RU361275};
KW Cytoplasm {ECO:0000256|RuleBase:RU361275};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000230750}.
FT DOMAIN 3..398
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 527..653
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 724 AA; 79452 MW; 82261515635B13E1 CRC64;
MLIVPPGSGI VHQVNLEYLA RVVFSSEGVL YPDSLVGTDS HTTMINGLGV VGWGVGGIEA
EAVMLGQPIS MVLPKVVGYK LHGQMNPLAT STDVVLTITK HLRQIGVVGK FVEFFGPGVA
QLSIADRATI ANMCPEYGAT VGFFPVDGNS LQYLRQTGRD EVKINIVESY LKANNLFRDF
TNPDQDPEFS EIYELDLASV KSCVSGPKRP HEKVMVSEMK EDFQTCLDNK IGFKGFNIPK
DKQISKVPFV YDNKEYTLTH GDVVIAAITS CTNTSNPSVM LGAGILAKKA VEAGLSVKPY
IKTSLSPGSG VVTYYLQDSG VIPYLEKLGF FIVGYGCMTC IGNSGPLDDS VAEPIEKGDL
VVCGVLSGNR NFEGRIHPLT RANYLASPPL VIAYAIAGTV SIDFETQPIG QSPDGKNVFL
RDIWPTRNEI QEVERQYVIP AMFKEVYAKI EKGNNRWNEL DAPESKLYPW DSQSTYIKSP
PFFETMEKDL PLVKNLCNAR PLLFLGDSVT TDHISPAGSI ARNSPAARYL SSRGLVPREF
NSYGSRRGND AIMARGTFAN IRLLNKFIGK AAPRTIHIPS NDIMDVFDAA ARYKEEGTPL
IIIAGKDYGS GSSRDWAAKG PWMQGIKAVI AESYERIHRS NLVGMGIIPL QFLDGQGAET
LGLTGREIYS IELPENIQPG QTVTVKMDNE KSFETTMRFD TDVELTYFRN GGILNYMIRH
LLEA
//
