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Database: UniProt
Entry: A0A067EHL2_CITSI
LinkDB: A0A067EHL2_CITSI
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ID   A0A067EHL2_CITSI        Unreviewed;       896 AA.
AC   A0A067EHL2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Aconitate hydratase {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU361275};
DE            Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU361275};
GN   ORFNames=CISIN_1g001917mg {ECO:0000313|EMBL:KDO54659.1};
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO54659.1, ECO:0000313|Proteomes:UP000027120};
RN   [1] {ECO:0000313|EMBL:KDO54659.1, ECO:0000313|Proteomes:UP000027120}
RP   NUCLEOTIDE SEQUENCE.
RG   International Citrus Genome Consortium;
RA   Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA   Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA   Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC       aconitate. {ECO:0000256|RuleBase:RU361275}.
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         ECO:0000256|RuleBase:RU361275};
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, ECO:0000256|RuleBase:RU361275}.
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DR   EMBL; KK784993; KDO54659.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067EHL2; -.
DR   Proteomes; UP000027120; Unassembled WGS sequence.
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   GO; GO:0043436; P:oxoacid metabolic process; IEA:UniProt.
DR   CDD; cd01586; AcnA_IRP; 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; 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   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW   Lyase {ECO:0000256|RuleBase:RU361275};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027120}.
FT   DOMAIN          163..666
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          795..891
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   896 AA;  97759 MW;  6379AD50B9BECD42 CRC64;
     MYITTSTSAA SSILRASSRS RFVSSLSSFK SLPARSLSPS PSSLVSQRSL GFASAVRSFR
     CSVPRWSHRV DWRSPLSLRA QIRTVAPAIE RLERAFATMA AEHPFKEILT ALPKPGGGEF
     GKFYSLPALN DPRIEKLPYS IRILLESAIR NCDNFQVKKE DVEKIIDWEN SAPKQVEIPF
     KPARVLLQDF TGVPAVVDLA CMRDAMNKLG SDSNKINPLV PVDLVIDHSV QVDVTRSENA
     VKANMELEFQ RNKERFAFLK WGSSAFHNML VVPPGSGIVH QVNLEYLGRV VFNTNGMLYP
     DSVVGTDSHT TMIDGLGVAG WGVGGIEAEA AMLGQPMSMV LPGVVGFKLS GKLHNGVTAT
     DLVLTVTQML RKHGVVGKFV EFHGDGMGEL SLADRATIAN MSPEYGATMG FFPVDHVTLQ
     YLKLTGRSDE TVAMVEGYLR ANKMFVDYNE PQQERVYSSY LELNLADVEP CISGPKRPHD
     RVPLKEMKAD WHSCLDNKVG FKGFAVPKET QEKVVKFSFH GQPAELKHGS VVIAAITSCT
     NTSNPSVMLG AGLVAKKACE LGLQVKPWVK TSLAPGSGVV TKYLLQSGLQ KYLNEQGFHI
     VGYGCTTCIG NSGDLDESVA STITDNDIVA AAVLSGNRNF EGRVHPLTRA NYLASPPLVV
     AYALAGTVDI DFDKEPIGTT KDGKSVYFKD IWPTTEEIAE VVQSSVLPDM FKSTYEAITK
     GNPTWNQLSV PASKLYSWDP NSTYIHEPPY FKDMTMDPPG AHGVKDAYCL LNFGDSITTD
     HISPAGSIHK DSPTAKYLLE RGVERRDFNS YGSRRGNDEV MARGTFANIR LVNKLLNGEV
     GPKTVHVPTG EKLSVFDAAM KYKSAGHGTI ILAGAEYGSG SSRDWAAKGP MLELKQ
//
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