ID A0A150FBW2_9BACI Unreviewed; 908 AA.
AC A0A150FBW2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-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=AXI58_13145 {ECO:0000313|EMBL:KXZ21873.1};
OS Bacillus nakamurai.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1793963 {ECO:0000313|EMBL:KXZ21873.1, ECO:0000313|Proteomes:UP000075430};
RN [1] {ECO:0000313|EMBL:KXZ21873.1, ECO:0000313|Proteomes:UP000075430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-41092 {ECO:0000313|EMBL:KXZ21873.1,
RC ECO:0000313|Proteomes:UP000075430};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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:KXZ21873.1}.
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DR EMBL; LSBA01000006; KXZ21873.1; -; Genomic_DNA.
DR RefSeq; WP_061521225.1; NZ_LSBA01000006.1.
DR AlphaFoldDB; A0A150FBW2; -.
DR STRING; 1793963.AXI58_13145; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000075430; 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; 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 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 82..577
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 707..834
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 908 AA; 99202 MW; C5DC4C1FA68D18FF CRC64;
MTNQQKVATQ DVFQAKKTFS SNGKTYHYYS LKALEDAGVG NVSKLPYSIK VLLESVLRQV
DGRVITKEHV ENLAKWGTAE LKDIDVPFKP SRVILQDFTG VPAVVDLASL RKAMASVGGD
PDKINPEIPV DLVIDHSVQV DKAGTEDALA INMDLEFERN AERYKFLSWA KKAFNNYQAV
PPATGIVHQV NLEFLASVVH TKDEDGELVT YPDTLVGTDS HTTMINGIGV LGWGVGGIEA
EAGMLGQPSY FPVPEVIGAK LVGKLPNGTT ATDLALKVTQ VLREKGVVNK FVEFFGPGVA
ELPLADRATI ANMAPEYGAT CGFFPVDEEA LAYLRLTGRD EEQIDVVEAY CRNNGLFFTP
DAEEPSFTDI VEIDLSKIEA NLSGPKRPQD LIPLSVMQET FKNHLVSPAG NQGFGLEAAE
ANKEISFKLL NGEETVMKTG AIAIAAITSC TNTSNPYVLI GAGLVAKKAV ELGLTVPNYV
KTSLAPGSKV VTGYLVNSGL LPYMKELGFN LVGYGCTTCI GNSGPLSPEI EEAVTENDLL
ITSVLSGNRN FEGRIHPLVK GNYLASPPLV VAYALAGTVN INLKSDPIGV GKDGQNVYFD
DIWPSMDEIN SLVKQTVTPE LFRKEYETVF DDNQRWNEIE TTDEALYKWD NDSTYIQNPP
FFEEMSVEPG KVEPLKALRV VGKFGDSVTT DHISPAGAIG KDTPAGKYLQ EKGVSPRDFN
SYGSRRGNHE VMMRGTFANI RIKNQIAPGT EGGYTTYWPT GEVTSIYDAC MRYKEDKTGL
VVLAGKDYGM GSSRDWAAKG TNLLGIRTVI AESFERIHRS NLVFMGVLPL QFKQGESADT
LGLTGKEVIE VDVDESVRPR DLLTVRAISE DGTVKTFEVI VRFDSEVEID YYRHGGILQM
VLRDKMKQ
//
