ID Q9VGZ3_DROME Unreviewed; 899 AA. AC Q9VGZ3; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 10-FEB-2021, entry version 155. DE RecName: Full=Citrate hydro-lyase {ECO:0000256|ARBA:ARBA00020648}; DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926}; DE AltName: Full=Cytoplasmic aconitate hydratase {ECO:0000256|ARBA:ARBA00020255}; DE AltName: Full=Iron-responsive element-binding protein 1 {ECO:0000256|ARBA:ARBA00015380}; GN Name=Irp-1B {ECO:0000313|EMBL:AAF54529.1, GN ECO:0000313|FlyBase:FBgn0024957}; GN Synonyms=144037_at {ECO:0000313|EMBL:AAF54529.1}, C-Acon GN {ECO:0000313|EMBL:AAF54529.1}, cACON {ECO:0000313|EMBL:AAF54529.1}, GN cAcon {ECO:0000313|EMBL:AAF54529.1}, dIRP GN {ECO:0000313|EMBL:AAF54529.1}, Dmel\CG6342 GN {ECO:0000313|EMBL:AAF54529.1}, IRF {ECO:0000313|EMBL:AAF54529.1}, IRP GN {ECO:0000313|EMBL:AAF54529.1}, IRP-1 {ECO:0000313|EMBL:AAF54529.1}, GN IRP-1B {ECO:0000313|EMBL:AAF54529.1}, irp-1B GN {ECO:0000313|EMBL:AAF54529.1}, IRP1 {ECO:0000313|EMBL:AAF54529.1}, GN IRP1B {ECO:0000313|EMBL:AAF54529.1}, irp1B GN {ECO:0000313|EMBL:AAF54529.1}; GN ORFNames=CG6342 {ECO:0000313|EMBL:AAF54529.1, GN ECO:0000313|FlyBase:FBgn0024957}, Dmel_CG6342 GN {ECO:0000313|EMBL:AAF54529.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF54529.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAF54529.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:AAF54529.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster RT euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AAF54529.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., Harris N.L., RA Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., RA Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:AAF54529.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., RA Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: a RT genomics perspective."; RL Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002). RN [5] {ECO:0000313|EMBL:AAF54529.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AAF54529.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:AAF54529.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."; RL Science 316:1586-1591(2007). RN [8] {ECO:0000313|EMBL:AAF54529.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis- CC aconitate. {ECO:0000256|ARBA:ARBA00003113}. 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 -!- COFACTOR: CC Note=Binds 1 [4Fe-4S] cluster per subunit. CC {ECO:0000256|RuleBase:RU361275}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|RuleBase:RU361275}. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014297; AAF54529.1; -; Genomic_DNA. DR RefSeq; NP_524303.2; NM_079579.3. DR SMR; Q9VGZ3; -. DR IntAct; Q9VGZ3; 1. DR STRING; 7227.FBpp0081736; -. DR PaxDb; Q9VGZ3; -. DR PRIDE; Q9VGZ3; -. DR EnsemblMetazoa; FBtr0082259; FBpp0081736; FBgn0024957. DR GeneID; 41269; -. DR KEGG; dme:Dmel_CG6342; -. DR UCSC; CG6342-RA; d. melanogaster. DR CTD; 41269; -. DR FlyBase; FBgn0024957; Irp-1B. DR eggNOG; KOG0452; Eukaryota. DR GeneTree; ENSGT00940000167487; -. DR HOGENOM; CLU_013476_2_1_1; -. DR InParanoid; Q9VGZ3; -. DR OMA; AFGEFQW; -. DR OrthoDB; 190960at2759; -. DR PhylomeDB; Q9VGZ3; -. DR Reactome; R-DME-917937; Iron uptake and transport. DR BioGRID-ORCS; 41269; 0 hits in 3 CRISPR screens. DR GenomeRNAi; 41269; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0024957; Expressed in arthropod fat body and 38 other tissues. DR ExpressionAtlas; Q9VGZ3; baseline and differential. DR Genevisible; Q9VGZ3; DM. DR GO; GO:0005829; C:cytosol; IMP:FlyBase. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0003994; F:aconitate hydratase activity; IDA:FlyBase. DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro. DR GO; GO:0006101; P:citrate metabolic process; IBA:GO_Central. DR GO; GO:0010040; P:response to iron(II) ion; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central. DR CDD; cd01580; AcnA_IRP_Swivel; 1. DR Gene3D; 3.20.19.10; -; 1. DR Gene3D; 3.30.499.10; -; 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 InterPro; IPR029784; IRE-BP1. DR PANTHER; PTHR11670; PTHR11670; 1. DR PANTHER; PTHR11670:SF32; PTHR11670:SF32; 1. DR Pfam; PF00330; Aconitase; 1. DR Pfam; PF00694; Aconitase_C; 1. DR PRINTS; PR00415; ACONITASE. DR SUPFAM; SSF53732; SSF53732; 1. DR TIGRFAMs; TIGR01341; aconitase_1; 1. DR PROSITE; PS00450; ACONITASE_1; 1. DR PROSITE; PS01244; ACONITASE_2; 1. PE 1: Evidence at protein level; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU361275}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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:0000313|EMBL:AAF54529.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Proteomics identification {ECO:0000213|PeptideAtlas:Q9VGZ3}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}. FT DOMAIN 77..574 FT /note="Aconitase" FT /evidence="ECO:0000259|Pfam:PF00330" FT DOMAIN 703..829 FT /note="Aconitase_C" FT /evidence="ECO:0000259|Pfam:PF00694" SQ SEQUENCE 899 AA; 98578 MW; 8F97C67B40DB680E CRC64; MSGANPFAQF EKTFSQAGTT YKYFDLASID SKYDQLPYSI RVLLESAVRN CDNFHILEKD VQSILGWSPA LKQGSNDVEV SFKPARVILQ DFTGVPAVVD FAAMRDAVLD LGGDPEKINP ICPADLVIDH SVQVDFARAP DALAKNQSLE FERNKERFTF LKWGAKAFNN MLIVPPGSGI VHQVNLEYLA RVVFENDATD GSKILYPDSV VGTDSHTTMI NGLGVLGWGV GGIEAEAVML GQSISMLLPE VIGYKLEGKL SPLVTSTDLV LTITKHLRQL GVVGKFVEFY GPGVAELSIA DRATISNMCP EYGATVGYFP IDENTLGYMK QTNRSEKKID IIRQYLKATQ QLRNYADAAQ DPKFTQSITL DLSTVVTSVS GPKRPHDRVS VSDMPEDFKS CLSSPVGFKG FAIAPEAQSA FGEFQWDDGK TYKLHHGSVV IAAITSCTNT SNPSVMLGAG LLAKKAVEKG LSILPYIKTS LSPGSGVVTY YLKESGVIPY LEKLGFDIVG YGCMTCIGNS GPLEENVVNT IEKNGLVCAG VLSGNRNFEG RIHPNTRANY LASPLLVIAY AIAGRVDIDF EKEPLGVDAN GKNVFLQDIW PTRSEIQEVE NKHVIPAMFQ EVYSKIELGS QDWQTLQVSE GKLFSWSADS TYIKRPPFFE GMTRDLPKLQ SIQKARCLLF LGDSVTTDHI SPAGSIARTS PAARFLSERN ITPRDFNSYG SRRGNDAIMS RGTFANIRLV NKLVEKTGPR TVHIPSQEEL DIFDAAERYR EEGTPLVLVV GKDYGSGSSR DWAAKGPFLL GVKAVIAESY ERIHRSNLVG MGIIPLQFLP GQSAETLNLT GREVYNIALP ESGLKPGQKI QVEADGTVFE TILRFDTEVD ITYYKNGGIL NYMIRKMLS //