ID E8PNW0_THESS Unreviewed; 901 AA.
AC E8PNW0;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 Name=acnA {ECO:0000313|EMBL:ADW21506.1};
GN OrderedLocusNames=TSC_c08810 {ECO:0000313|EMBL:ADW21506.1};
OS Thermus scotoductus (strain ATCC 700910 / SA-01).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=743525 {ECO:0000313|EMBL:ADW21506.1, ECO:0000313|Proteomes:UP000008087};
RN [1] {ECO:0000313|Proteomes:UP000008087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RA Gounder K., Liesegang H., Brzuszkiewicz E., Wollherr A., Daniel R.,
RA Gottschalk G., van Heerden E., Litthauer D.;
RT "The genome sequence of Thermus scotoductus SA-01.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADW21506.1, ECO:0000313|Proteomes:UP000008087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700910 / SA-01 {ECO:0000313|Proteomes:UP000008087};
RX PubMed=22115438; DOI=10.1186/1471-2164-12-577;
RA Gounder K., Brzuszkiewicz E., Liesegang H., Wollherr A., Daniel R.,
RA Gottschalk G., Reva O., Kumwenda B., Srivastava M., Bricio C.,
RA Berenguer J., van Heerden E., Litthauer D.;
RT "Sequence of the hyperplastic genome of the naturally competent Thermus
RT scotoductus SA-01.";
RL BMC Genomics 12:577-577(2011).
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 -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; CP001962; ADW21506.1; -; Genomic_DNA.
DR RefSeq; WP_015716783.1; NC_014974.1.
DR AlphaFoldDB; E8PNW0; -.
DR STRING; 743525.TSC_c08810; -.
DR KEGG; tsc:TSC_c08810; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_0; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000008087; 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.
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}.
FT DOMAIN 76..568
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 696..822
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 901 AA; 99045 MW; 2480BF135C080CF8 CRC64;
MKDSFQTLKT LNTPSGTYAY FDLTELERKG IAEVSRLPFS IRIMLESLLR NEDGYQVTRE
DIEALARWTP EPGEINVPLK LARVILQDFT GVPAVVDLAA MRDAVAERGG DPKRINPVVP
ADLVIDHSVQ VDAFGTAYAF FYNVEKEYER NRERYLLLKW AQGALENFRV VPPGTGIVHQ
VNLEYLAKVV MTKEEGGLTL AFPDSLVGTD SHTTMVNGLG VLGWGVGGIE AEAVMLGQPY
YMLAPKVVGF KLYGELPEGA TATDLVLTIT EILRKHGVVG KFVEFYGPGV AKLSLADRAT
IANMAPEYGA TMGFFPVDEE TLNYLRLTGR PEELIALVEA YTKANGLFRT PEAEERVRYS
EYLELDLSTV EPSLAGPKRP QDRVALKEVK QSFLAHLTKP VKERGFGLTP DQLNKKVLVK
RQDEEFELTH GSVVIAAITS CTNTSNPTVM LGAGLLAKKA VEAGLDTKPW VKSSLAPGSK
VVTDYLEASG LLPFLEALRF HVVGYGCTTC IGNSGPLPED IAKAVEEGNL VVAAVLSGNR
NFEGRINPHV KANYLASPML VVAYALAGRM DIDFTTEPLG YDPNGKPVYL KDIWPSMEEI
REAMAKTLDP GLFKKEYAKV FEGDERWQAL PAPTGELFGW DPESTYIQKP PFFQNLGQHQ
VGDIRGARVL LVLGDSVTTD HISPAGAIPV KSPAGQYLIS KGVKPEDFNS YGSRRGNHEV
MVRGTFANIR IKNLMLDGIE GGYAKKLPEG EVDFVYHVAM RYQEEGTPLL VIAGKEYGTG
SSRDWAAKGT YLLGIKAVLA ESFERIHRSN LVGMGVLPLE FLPGENRETL GLTGYEVYDI
LGLEDLTPRK KVEVVARKED GTEVRFQAIA RLDTPVEVDY YKNGGILQTV LLNMLKEAKA
Q
//
