ID A0A0N1FW02_9ACTN Unreviewed; 904 AA.
AC A0A0N1FW02;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=OV450_4223 {ECO:0000313|EMBL:KPI04595.1};
OS Actinobacteria bacterium OV450.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592328 {ECO:0000313|EMBL:KPI04595.1, ECO:0000313|Proteomes:UP000037826};
RN [1] {ECO:0000313|EMBL:KPI04595.1, ECO:0000313|Proteomes:UP000037826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV450 {ECO:0000313|EMBL:KPI04595.1,
RC ECO:0000313|Proteomes:UP000037826};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-2015) 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=(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 ECO:0000256|RuleBase:RU361275};
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, ECO:0000256|RuleBase:RU361275}.
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:KPI04595.1}.
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DR EMBL; LJCW01000339; KPI04595.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1FW02; -.
DR PATRIC; fig|1592328.3.peg.6807; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000037826; Unassembled WGS sequence.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
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: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 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, ECO:0000313|EMBL:KPI04595.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 64..572
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 702..831
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 398..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 97149 MW; 52F973A41FA994F2 CRC64;
MSANSFDARS TLQVGDESYE IFRLDKVEGS ARLPYSLKVL LENLLRTEDG ANITADHIRS
LGNWDSQAQP SEEIQFTPAR VIMQDFTGVP CVVDLATMRE AVKALGGDPA KINPLSPAEM
VIDHSVIADK FGTKDAFAQN VELEYGRNKE RYQFLRWGQT AFDDFKVVPP GTGIVHQVNI
EHLARTVMVR NGQAYPDTLV GTDSHTTMVN GLGVLGWGVG GIEAEAAMLG QPVSMLIPRV
VGFKLTGELP TGTTATDLVL TITEMLRKHG VVGKFVEFYG EGVAATSLAN RATIGNMSPE
FGSTAAIFPI DGETLKYLRL TGRDAQQVAL VEAYAKEQGL WLAPAAEPDF SEKLELDLST
VVPSIAGPKR PQDRIVLANA AEQFAVDVRN YVSDDEEAGK ESFPASDAPA AVNGVPTRPT
QVTLADGTSF EIDHGAVTVA AITSCTNTSN PYVMVAAALV AKKAVEKGLS RKPWVKTTLA
PGSKVVTDYF DKAGLTPYLD KMGFNLVGYG CTTCIGNSGP LDEEISKAIN EHDLAVTSVL
SGNRNFEGRI NPDVKMNYLA SPPLVVAYAI AGSMKVDITK DAIGIDTEGK PVFLQDIWPS
EAEVNDVVAN AIGEDMFSKS YQDVFAGDAQ WQALSIPTGN TFEWDPQSTY VRKPPYFEGM
TMETTPVSDI AGARVLAKLG DSVTTDHISP AGAIKADTPA GKYLTEHGVE RRDFNSYGSR
RGNHEVMIRG TFANIRLRNQ IAPGTEGGFT RDFTVEGAPV AFIYDASQNY QAAGIPLVIL
AGKEYGSGSS RDWAAKGTAL LGVKAVIAES YERIHRSNLI GMGVLPLQFP EGASAAALGL
TGEETFSFTG VEELNNGTTP RTVKVTTDTG VEFDAVVRID TPGEADYYRN GGIMQYVLRN
LIRG
//