ID A0A0M4FWB1_9BACI Unreviewed; 907 AA.
AC A0A0M4FWB1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=AM592_05795 {ECO:0000313|EMBL:ALC81163.1};
OS Bacillus gobiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1441095 {ECO:0000313|EMBL:ALC81163.1, ECO:0000313|Proteomes:UP000067625};
RN [1] {ECO:0000313|Proteomes:UP000067625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-4402 {ECO:0000313|Proteomes:UP000067625};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALC81163.1, ECO:0000313|Proteomes:UP000067625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-4402 {ECO:0000313|EMBL:ALC81163.1,
RC ECO:0000313|Proteomes:UP000067625};
RX PubMed=26530456; DOI=10.1099/ijsem.0.000729;
RA Liu B., Liu G.H., Cetin S., Schumann P., Pan Z.Z., Chen Q.Q.;
RT "Bacillus gobiensis sp. nov., isolated from a soil sample.";
RL Int. J. Syst. Evol. Microbiol. 66:379-384(2016).
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; CP012600; ALC81163.1; -; Genomic_DNA.
DR RefSeq; WP_053602913.1; NZ_CP012600.1.
DR AlphaFoldDB; A0A0M4FWB1; -.
DR STRING; 1441095.AM592_05795; -.
DR PATRIC; fig|1441095.3.peg.1262; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000067625; 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:ALC81163.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000067625};
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 907 AA; 99262 MW; AC238B5FE9748B76 CRC64;
MANQQKLVKN DVFQARKSFT VNGKTYYYYS LKALEEQGAG KVSRLPYSIK VLLESVLRQV
DGKVITKEHV ENLAKWGTSD VKEIDVPFKP SRVILQDFTG VPAVVDLASL RKAMDSVGGD
PDKINPEIPV DLVIDHSVQV DKAGTEDALA INMDLEFERN EERYKFLSWA KKAFDNYQAV
PPATGIVHQV NLEYLASVVH EQEIDGETVT YPDSLVGTDS HTTMINGIGV LGWGVGGIEA
EAGMLGQPSY FPVPEVIGAK LVGKLPNGTT ATDLALKVTQ VLREKGVVGK FVEFYGPGVA
ELPLADRATI ANMAPEYGAT CGFFPVDDEA LVYMKLTGRE DKHIDVVKEY CIQNGLFYTP
DAEEPEFTDT VEINLSEIEA NLSGPKRPQD LIPLSAMKET FHNHLTSAAG NQGFGLEADE
INKEVKFKLA SGKETVMKTG AIAIAAITSC TNTSNPYVLV GAGLVAKKAT ELGMQVPDYV
KTSLAPGSKV VTGYLVNSGL LPYLRELGFN LVGYGCTTCI GNSGPLEQEI EEAVAESDLL
ITSVLSGNRN FEGRIHPLVK GNYLASPPLV VAYALAGTVD IDLKTDPIGV DKDGKDVYFD
DIWPTMDEIN QVVNQTVTPE LFKKEYEHVF DDNQRWNEIE TTDEALYKWD TESTYIQNPP
FFENLSVEPG TVEPLKGLRV VGKFGDSVTT DHISPAGAIG KDTPAGKYLQ SKGVSPRDFN
SYGSRRGNHE VMMRGTFANI RIKNQIAPGT EGGYTTFWPT GEVTSIYEAC MKYKEEGTGL
AVLAGKDYGM GSSRDWAAKG TNLLGIKTVI AESFERIHRS NLVLMGVLPL QFKQGENAEV
LGLTGKETIE VDIDETVKPR DIVTVRATSE QGEVTSFEAL VRFDSEIEID YYRHGGILQM
VLREKLK
//
