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Database: UniProt
Entry: A0A0A8X4L8_9BACI
LinkDB: A0A0A8X4L8_9BACI
Original site: A0A0A8X4L8_9BACI 
ID   A0A0A8X4L8_9BACI        Unreviewed;       902 AA.
AC   A0A0A8X4L8;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=SAMD00020551_1233 {ECO:0000313|EMBL:GAM13096.1};
OS   Mesobacillus selenatarsenatis SF-1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=1321606 {ECO:0000313|EMBL:GAM13096.1, ECO:0000313|Proteomes:UP000031014};
RN   [1] {ECO:0000313|EMBL:GAM13096.1, ECO:0000313|Proteomes:UP000031014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF-1 {ECO:0000313|EMBL:GAM13096.1,
RC   ECO:0000313|Proteomes:UP000031014};
RA   Kuroda M., Sei K., Yamashita M., Ike M.;
RT   "Whole genome shotgun sequence of Bacillus selenatarsenatis SF-1.";
RL   Submitted (JUN-2013) 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|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   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:GAM13096.1}.
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DR   EMBL; BASE01000025; GAM13096.1; -; Genomic_DNA.
DR   RefSeq; WP_041964972.1; NZ_BASE01000025.1.
DR   AlphaFoldDB; A0A0A8X4L8; -.
DR   STRING; 1321606.SAMD00020551_1233; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000031014; 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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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: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:GAM13096.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031014};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          76..571
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          701..828
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   902 AA;  98622 MW;  A41D6DF8D94442BD CRC64;
     MSNQDVFNAR SSFEVDGKRY HYYSLAALEK AGIGNVSKLP YSVKVLLESV LRQHDGFVIT
     KEHVENLAKW GTSEVKEVDV PFKPSRVILQ DFTGVPAVVD LASLRKAMAD MGGDPQKINP
     EKPVDLVIDH SVQVDKYGTP DALNVNMELE FERNAERYQF LSWAQKAFDN YRAVPPATGI
     VHQVNLEYLA NVVHAVENAD GEFETFPDSL VGTDSHTTMI NGIGVLGWGV GGIEAEAGML
     GQPSYFPVPE VVGVKLVGDM PNGATATDLA LKVTQVLRSK GVVGKFVEFF GPGVVTLPLA
     DRATVANMAP EYGATCGFFP VDGEALDYMR LTGRTEDHIK VVEAYCKENG LFFDPALEPV
     YTDVVEINLS EIEANLSGPK RPQDLIPLSD MQKSFKEALT APAGNQGFGL DKKEIEKEAV
     VEFANGDKTT MKTGAIAIAA ITSCTNTSNP YVLVGAGLVA KKAVELGMEV PKFVKTSLAP
     GSKVVTGYLR DSELLPYLET LGFNLVGYGC TTCIGNSGPL KPEIEKSVAE SDLLVTSVLS
     GNRNFEGRIH PLVKANYLAS PPLVVAYALA GTVDVDLQND PIGKDKDGND VFFKDIWPST
     EEVNEVVHRV VTPELFRREY ETVFTDNEKW NEIQTNSDPL YTFDEDSTYI ANPPFFEGLT
     PEAGEVAPLN NLRIVGKFGD SVTTDHISPA GAIGKDTPAG KYLREKGVEP RDFNSYGSRR
     GNHEVMMRGT FANIRIKNQI APGTEGGFTT YWPTNEVMSI FDACMKYKEQ GTGLMVIAGK
     DYGMGSSRDW AAKGTNLLGI KTVIAESFER IHRSNLVLMG VLPLQFKAGE NAETLGLTGR
     ESFDVQIDEK VRPRDIITVT ATDEDGNKKT FEALVRFDSE VEIDYYRHGG ILQMVLRDKL
     KA
//
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