ID A0A067ETX2_CITSI Unreviewed; 996 AA.
AC A0A067ETX2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-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:KDO54657.1};
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:KDO54657.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO54657.1, 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; KDO54657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067ETX2; -.
DR STRING; 2711.A0A067ETX2; -.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0003994; F:aconitate hydratase activity; IBA:GO_Central.
DR GO; GO:0030350; F:iron-responsive element binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006101; P:citrate metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR CDD; cd01586; AcnA_IRP; 1.
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; CITRATE HYDRO-LYASE; 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..923
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 996 AA; 108691 MW; 5B699E235363D0C4 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 MLLVIKAVIA
KSFERIHRSN LVGMGIIPLC FKAGEDADSL GLTGHERFSI DLPSKISEIR PGQDVTVTTD
SGKSFTCTVR FDTEVELAYF DHGGILPFVI RNLIKQ
//