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
//