ID N0AZH1_9BACI Unreviewed; 908 AA.
AC N0AZH1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=B1NLA3E_10615 {ECO:0000313|EMBL:AGK53881.1};
OS Bacillus sp. 1NLA3E.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK53881.1, ECO:0000313|Proteomes:UP000013300};
RN [1] {ECO:0000313|EMBL:AGK53881.1, ECO:0000313|Proteomes:UP000013300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLA3E {ECO:0000313|EMBL:AGK53881.1};
RX PubMed=23833140;
RA Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA Brooks S., Kostka J.E., Green S.J.;
RT "Genome sequences for three denitrifying bacterial strains isolated from a
RT uranium- and nitrate-contaminated subsurface environment.";
RL Genome Announc. 1:e00449-13(2013).
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}.
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DR EMBL; CP005586; AGK53881.1; -; Genomic_DNA.
DR RefSeq; WP_015593939.1; NC_021171.1.
DR AlphaFoldDB; N0AZH1; -.
DR STRING; 666686.B1NLA3E_10615; -.
DR KEGG; baci:B1NLA3E_10615; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_9; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000013300; Chromosome.
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, ECO:0000313|EMBL:AGK53881.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000013300};
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; 98948 MW; A3AF50231CAAE41B CRC64;
MSKNEVLAKN DVFQARASFD LNGKKYNFYR LGALEDAGLG KISRLPYSIK VLLESVLRQY
DGRVITKEHV ENLAKWGTSE VKEVDVPFKP SRVILQDFTG VPAVVDLASL RKAMADMGGD
PDKINPEKTV DLVIDHSVQV DFYGSESALE ENMELEFERN AERYQFLSWA QKSFNNYRAV
PPATGIVHQV NLEYLADVVH VAQTEDGGFE AFPDTLVGTD SHTTMINGIG VLGWGVGGIE
AEAGMLGQPS YFPVPEVIGV KLVGELPNGA TATDLALKVT QVLRGAGVVN KFVEFFGPGV
SSLPLADRAT VANMAPEYGA TCGFFPIDGE SLEYLRLTGR NEESIKVVEQ YCKANGLFLN
PTDEPVYTKV VEIDLSIIEP NLSGPKRPQD LIPLSEMKET FVNAVSSPQG NQGFGLTAAE
LDREITVKFD NGDETVMKTG AIAIAAITSC TNTSNPYVLV GAGLVAKKAV ELGLQVPKFV
KTSLAPGSKV VTGYLRDSGL LPYLEKLGFN TVGYGCTTCI GNSGPLKEEI EKAVADSDLL
VTSVLSGNRN FEGRIHALVK GNYLASPPLV VAYALAGNVN VDLQKDVIGK DKDGNDVFFK
DIWPTTAEIN EIVKQNVTPE LFRKEYDNVF ADNARWNQIQ TSNEPLYTWD EESTYIANPP
FFEGLKPDPE EVKPLTGLRV VGKFGDSVTT DHISPAGSIG KNTPAGKYLT EKGVAPRDFN
SYGSRRGNHE VMMRGTFANI RIRNQIAPGT EGGVTTYWPT GEVTSIFDAC MQYKQDGTGL
AILAGKDYGM GSSRDWAAKG TNLLGIKTVI AESFERIHRS NLVLMGVLPL QFKQGESAET
LGLTGKEAID VLVDETVKPR DFVKVTATDE AGNKKEFEVL VRFDSEVEID YYRHGGILQM
VLREKIKG
//