ID   Q9VGZ3_DROME            Unreviewed;       899 AA.
AC   Q9VGZ3;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-NOV-2024, entry version 170.
DE   SubName: Full=Iron regulatory protein 1B {ECO:0000313|EMBL:AAF54529.1};
DE            EC=4.2.1.3 {ECO:0000313|EMBL:AAF54529.1};
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; Endopterygota; 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|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|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., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., 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|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:RESEARCH0084.1-RESEARCH0084.20(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   -!- 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}.
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DR   EMBL; AE014297; AAF54529.1; -; Genomic_DNA.
DR   RefSeq; NP_524303.2; NM_079579.3.
DR   AlphaFoldDB; Q9VGZ3; -.
DR   SMR; Q9VGZ3; -.
DR   IntAct; Q9VGZ3; 1.
DR   STRING; 7227.FBpp0081736; -.
DR   PaxDb; 7227-FBpp0081736; -.
DR   DNASU; 41269; -.
DR   EnsemblMetazoa; FBtr0082259; FBpp0081736; FBgn0024957.
DR   GeneID; 41269; -.
DR   KEGG; dme:Dmel_CG6342; -.
DR   UCSC; CG6342-RA; d. melanogaster.
DR   AGR; FB:FBgn0024957; -.
DR   CTD; 41269; -.
DR   FlyBase; FBgn0024957; Irp-1B.
DR   VEuPathDB; VectorBase:FBgn0024957; -.
DR   eggNOG; KOG0452; Eukaryota.
DR   GeneTree; ENSGT00940000167487; -.
DR   HOGENOM; CLU_013476_2_1_1; -.
DR   InParanoid; Q9VGZ3; -.
DR   OMA; NGGIMQY; -.
DR   OrthoDB; 176941at2759; -.
DR   PhylomeDB; Q9VGZ3; -.
DR   Reactome; R-DME-389542; NADPH regeneration.
DR   Reactome; R-DME-917937; Iron uptake and transport.
DR   BioGRID-ORCS; 41269; 0 hits in 3 CRISPR screens.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0024957; Expressed in crop (Drosophila) and 146 other cell types or tissues.
DR   ExpressionAtlas; Q9VGZ3; baseline and differential.
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: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   FunFam; 3.20.19.10:FF:000001; Aconitate hydratase; 1.
DR   FunFam; 3.30.499.10:FF:000002; Aconitate hydratase; 1.
DR   FunFam; 3.30.499.10:FF:000005; cytoplasmic aconitate hydratase; 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   1: Evidence at protein level;
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   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AAF54529.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q9VGZ3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803}.
FT   DOMAIN          74..574
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          703..829
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
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
//