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Database: UniProt
Entry: A0A021VRP2_9CELL
LinkDB: A0A021VRP2_9CELL
Original site: A0A021VRP2_9CELL 
ID   A0A021VRP2_9CELL        Unreviewed;       947 AA.
AC   A0A021VRP2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE            EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE            EC=4.2.1.99 {ECO:0000256|ARBA:ARBA00013250};
DE   AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000256|ARBA:ARBA00031613};
DE   AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000256|ARBA:ARBA00030846};
DE   AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE   AltName: Full=Probable 2-methyl-cis-aconitate hydratase {ECO:0000256|ARBA:ARBA00033025};
DE   AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN   Name=acnA {ECO:0000313|EMBL:EYR63793.1};
GN   ORFNames=N866_18260 {ECO:0000313|EMBL:EYR63793.1};
OS   Actinotalea ferrariae CF5-4.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Actinotalea.
OX   NCBI_TaxID=948458 {ECO:0000313|EMBL:EYR63793.1, ECO:0000313|Proteomes:UP000019753};
RN   [1] {ECO:0000313|EMBL:EYR63793.1, ECO:0000313|Proteomes:UP000019753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF5-4 {ECO:0000313|EMBL:EYR63793.1,
RC   ECO:0000313|Proteomes:UP000019753};
RA   Chen F., Li Y., Wang G.;
RT   "Actinotalea ferrariae CF5-4.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC         aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC         Evidence={ECO:0000256|ARBA:ARBA00000118};
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   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000256|ARBA:ARBA00005026}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYR63793.1}.
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DR   EMBL; AXCW01000067; EYR63793.1; -; Genomic_DNA.
DR   RefSeq; WP_034225143.1; NZ_AXCW01000067.1.
DR   AlphaFoldDB; A0A021VRP2; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000019753; Unassembled WGS sequence.
DR   GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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   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   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000313|EMBL:EYR63793.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019753}.
FT   DOMAIN          71..613
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          743..870
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
FT   REGION          420..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..460
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   947 AA;  101633 MW;  D34101DD5411037E CRC64;
     MSSVDTFRSQ GRLEVGDTSY EIFRLSAVPG LERLPFSLKV LAENLLRTED GANVTAEHVR
     AIAAWDPAAE PSTEIQFTPA RVIMQDFTGV PCVVDLATMR EAVAELGGDP ARINPLAPAE
     LVIDHSVQID VAGRRDAFER NVELEYQRNR ERYQFLRWGQ TAFDDFKVVP PGTGIVHQVN
     LEYLARGVMT REVGGALRAY PDTCVGTDSH TTMVNGLGVL GWGVGGIEAE AAMLGQPVSM
     LIPRVVGFKL TGSIPAGVTA TDVVLTITEQ LRRHGVVGKF VEFYGAGVAE VPLANRATIG
     NMSPEFGSTC AIFPIDEVTL DYLRLTGRPA DQVALVEAYA QEQGLWHDPS SADYVEPTFS
     EYLELDLSTV VPSIAGPKRP QDRIELTEAK EAFASVILDY VDPDTAAAVR AARQVTDGLD
     ESVEETFPAS DPIAAGEHAD TSAAPREPGH ADAARRPHKR VPVTLADGTR TEIDHGSVVI
     ASITSCTNTS NPSVMLAAAL LAKKAVARGL TAKPWVKTSM APGSKVVTDY YQKAGLWPYL
     EKLGFHLVGY GCATCIGNSG PLPEEVSEVV NEHDLSVVSV LSGNRNFEGR INPDVKMNYL
     ASPPLVIAYA LAGTMDFDFE AEPLGTSETG EPVFLRDIWP SPQEVQATID SSIDSAMFTA
     DYADVFAGDE RWQTLPTPSG DTFAWDPEST YVRRPPYFEG MGMTPDPVTD IEGARVLAKL
     GDSVTTDHIS PAGSIKADSP AGRYLAEHGV DRRDFNSYGS RRGNHEVMIR GTFANIRLRN
     QLVPGVEGGV TVNHLTGEQT SIYDAAVAYA AAGVPLVVLG GKEYGSGSSR DWAAKGTRLL
     GVRAVVAESF ERIHRSNLIG MGVLPLQFPA GETADSLGLD GTETFAVSGV TALNEGTTPR
     TVAVRAEKAD GTVVEFDAVV RIDTPGEADY YRNGGILQYV LRSLVTS
//
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