ID A0A165Y334_9BACI Unreviewed; 908 AA.
AC A0A165Y334;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=AZI98_07665 {ECO:0000313|EMBL:KZN96676.1};
OS Aeribacillus pallidus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Aeribacillus.
OX NCBI_TaxID=33936 {ECO:0000313|EMBL:KZN96676.1, ECO:0000313|Proteomes:UP000076476};
RN [1] {ECO:0000313|EMBL:KZN96676.1, ECO:0000313|Proteomes:UP000076476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8m3 {ECO:0000313|EMBL:KZN96676.1,
RC ECO:0000313|Proteomes:UP000076476};
RA Poltaraus A.B., Nazina T.N., Tourova T.P., Malakho S.M., Korshunova A.V.,
RA Sokolova D.S.;
RT "Draft genome sequence of Aeribacillus pallidus 8m3 from petroleum
RT reservoir.";
RL Submitted (APR-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:KZN96676.1}.
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DR EMBL; LWBR01000017; KZN96676.1; -; Genomic_DNA.
DR RefSeq; WP_063387692.1; NZ_SFCD01000016.1.
DR STRING; 33936.AZI98_07665; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000076476; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076476};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 81..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; 99950 MW; 42E4A1E93F57B0B5 CRC64;
MSQQQLEKND VFRARKSFSI NGKTYNYYSL KALEDAGIGQ VSRLPYSIKV LLESVLRQVD
GRVITKEHVE NLAKWGTDEI KNLDVPFKPS RVILQDFTGV PAVVDLASLR KAMADMGGDP
QKINPEKPVD LVIDHSVQVD RAGTDDALQY NMNLEFERNA ERYKFLNWAQ KAFDNYRAVP
PATGIVHQVN LEYLASVVHA VEGENGEYET YPDTLVGTDS HTTMINGLGV LGWGVGGIEA
EAGMLGQPSY FPVPEVIGVR LVGELPNGTT ATDLALKVTQ VLRQKGVVGK FVEFFGPGVA
KLPLADRATI ANMAPEYGAT CGFFPVDNES LEYLRLTGRD EEHVKVVETY CKENGLFFTP
EAEDPIFTDV VEIDLSQIEA NLSGPKRPQD LIPLSKMKEE FHRALTAPQG NQGFGLQPEE
LNKEVTVEFA NGEKTTMKTG AVVIAAITSC TNTSNPYVLV GAGLVAKKAV EKGLTVPKYV
KTSLAPGSKV VTGYLQNSGL MPYLEKLGFN LVGYGCTTCI GNSGPLADEI EKAIAENDLL
VTSVLSGNRN FEGRIHPLVK GNYLASPPLV VAYALAGTVD IDLLNDPIGK DQNGSDVYFK
DIWPSMEEIN EVVKQTVTPE LFRKEYERVF DDNERWNAIE TTDEPLYQWD EESTYIQNPP
FFEGLSPEPG KVEPLKGLRV VGKFGDSVTT DHISPAGAIG KDTPAGQYLL SKGVSPRDFN
SYGSRRGNHE VMMRGTFANI RIRNQIAPGT EGGYTTYWPT GEVMSIYDAC MKYKQDGTGL
VVLAGKDYGM GSSRDWAAKG TNLLGIKTVI AESFERIHRS NLVLMGVLPL QFKEGENAET
LGLTGKEVLD VHIDESVKPR DYIKVTATDE NGNKKEFEVL VRFDSEVEID YYRHGGILQM
VLRERLKG
//