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Database: UniProt
Entry: A0A067FVH3_CITSI
LinkDB: A0A067FVH3_CITSI
Original site: A0A067FVH3_CITSI 
ID   A0A067FVH3_CITSI        Unreviewed;       898 AA.
AC   A0A067FVH3;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Aconitate hydratase {ECO:0000256|RuleBase:RU361275};
DE            Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE            EC=4.2.1.3 {ECO:0000256|RuleBase:RU361275};
GN   ORFNames=CISIN_1g002610mg {ECO:0000313|EMBL:KDO71343.1};
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:KDO71343.1, ECO:0000313|Proteomes:UP000027120};
RN   [1] {ECO:0000313|EMBL:KDO71343.1, 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|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; KK784889; KDO71343.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067FVH3; -.
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   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:SF62; ACONITATE HYDRATASE 1; 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          65..566
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          695..822
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   898 AA;  98347 MW;  053D294E83550E67 CRC64;
     MATENPFKSI LKTLQRPDGG EFGKYYSLPA LNDPRIDKLP YSIKILLESA IRNCDEFQVK
     SKDVEKIIDW ETTSPKQVEI PFKPARVLLQ DFTGVPAVVD LACMRDAMNK LGGDSNKINP
     LVPVDLVIDH SVQVDVARSE NAVQANMEFE FRRNKERFAF LKWGSNAFHN MLVVPPGSGI
     VHQVNLEYLG RVVFNTNGML YPDSVVGTDS HTTMIDGLGV AGWGVGGIEA EAAMLGQPMS
     MVLPGVVGFK LSGKLRDGVT ATDLVLTVTQ MLRKHGVVGM FVEFYGEGMS ELSLADRATI
     ANMSPEYGAT MGFFPVDHVT LQYLKLTGRS DDTVSMIESY LRANKMFVDY SESERVYSSY
     LELNLEEVVP CVSGPKRPHD RVPLNEMKAD WHACLDNRVG FKGFAIPKEY QSKVAEFNFH
     GTPAQLRHGD VVIAAITSCT NTSNPSVMLG AALVAKKACE LGLEVKPWIK TSLAPGSGVV
     TKYLQNSGLQ KYLNHLGFHI VGYGCTTCIG NSGDIDDAVA AAITENDIVA AAVLSGNRNF
     EGRVHPLTRA NYLASPPLVV AYALAGSVNI DFETEPVGVG KDGKKIFLRD IWPSSEEVAH
     VVQKSVLPDM FKATYEAITK GNPMWNQLSV PSGTLYAWDP KSTYIHEPPY FKDMTMSPPG
     PHGVKGAYCL LNFGDSITTD HISPAGSIHK DSPAAKYLME RGVDRRDFNS YGSRRGNDEI
     MARGTFANIR LVNKLLNGEV GPKTIHIPTG EKLSVFDAAM RYKNEGHDTV ILAGAEYGSG
     SSRDWAAKGP MLLGVKAVIA KSFERIHRSN LVGMGIIPLC FKPGEDAETH GLTGHERYTI
     DLPSSVSEIR PGQDVRVVTD SGKSFTCVIR FDTEVELAYF DHGGILQYVI RNLINVRQ
//
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