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Database: UniProt
Entry: C7R4J8_JONDD
LinkDB: C7R4J8_JONDD
Original site: C7R4J8_JONDD 
ID   C7R4J8_JONDD            Unreviewed;       917 AA.
AC   C7R4J8;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   24-JAN-2024, entry version 80.
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   OrderedLocusNames=Jden_1402 {ECO:0000313|EMBL:ACV09055.1};
OS   Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / BCRC 15368 / CIP
OS   55.134 / JCM 11481 / NBRC 15587 / NCTC 10816 / Prevot 55134) (Listeria
OS   denitrificans).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae;
OC   Jonesia.
OX   NCBI_TaxID=471856 {ECO:0000313|EMBL:ACV09055.1, ECO:0000313|Proteomes:UP000000628};
RN   [1] {ECO:0000313|EMBL:ACV09055.1, ECO:0000313|Proteomes:UP000000628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14870 / DSM 20603 / BCRC 15368 / CIP 55.134 / JCM 11481 /
RC   NBRC 15587 / NCTC 10816 / Prevot 55134
RC   {ECO:0000313|Proteomes:UP000000628};
RX   PubMed=21304666; DOI=10.4056/sigs.41646;
RA   Pukall R., Gehrich-Schroter G., Lapidus A., Nolan M., Glavina Del Rio T.,
RA   Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., Copeland A.,
RA   Saunders E., Brettin T., Detter J.C., Bruce D., Goodwin L., Pati A.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Han C.;
RT   "Complete genome sequence of Jonesia denitrificans type strain (Prevot
RT   55134).";
RL   Stand. Genomic Sci. 1:262-269(2009).
CC   -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC       aconitate. {ECO:0000256|RuleBase:RU361275}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC         aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC         Evidence={ECO:0000256|ARBA:ARBA00000118};
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   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000256|ARBA:ARBA00005026}.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR   EMBL; CP001706; ACV09055.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7R4J8; -.
DR   STRING; 471856.Jden_1402; -.
DR   KEGG; jde:Jden_1402; -.
DR   eggNOG; COG1048; Bacteria.
DR   HOGENOM; CLU_013476_2_1_11; -.
DR   OMA; NGGIMQY; -.
DR   UniPathway; UPA00223; UER00718.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000000628; Chromosome.
DR   GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
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; 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:UP000000628}.
FT   DOMAIN          70..584
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          713..840
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   917 AA;  99534 MW;  29FD08B2F3CEE841 CRC64;
     MSNVDTFKSK GTLDVQGTAY EIFRLNAVPG LERLPYSLKV LAENLLRTED GANITAEHIH
     ALANWDPTAQ PNTEIQFTPA RVIMQDFTGV PCVVDLATMR EAVVELGGDP SRINPLAPAE
     LVIDHSVQID VAGRRDAFER NVELEYERNR ERYQFLRWGQ TAFEEFKVVP PGTGIVHQVN
     IEYLARTVMT REVGGVLRAY PDTCVGTDSH TTMVNGLGVL GWGVGGIEAE AAMLGQSVSM
     LIPRVVGFKL TGSIPAGVTA TDVVLTITQM LRHHGVVGKF VEFYGAGVSQ VPLANRATIG
     NMSPEFGSTA AIFPIDDVTL DYLKLTGRST EQLALVEAYA KEQGLWLDPT DPSYIEPQFS
     EYLELDLSTV VPSIAGPKRP QDRIELTRAK EQFDRDLPNY VSTSANLIDE AEKESFPASD
     APAITDTTTS TVEVTDTNGK TFDLFNGAVA IASITSCTNT SNPSVMLAAA ILAKKAVERG
     LEAKPWVKTS MAPGSQVVTN YYEKAGLWPY LEKLGFHLVG YGCATCIGNS GPLDDNISAA
     VNEHDLAIVS VLSGNRNFEG RINPDVKMNY LASPPLVVAY ALAGTMSFDF DTEPLGFDTE
     GAPVFLKDIW PTPEEVQATI DSTIDRAMFE KDYADVFAGD DRWRSLPTPE GDTFAWDNES
     TYVRKPPYFD GMGAQPEPVN DIRTARVLAK LGDSVTTDHI SPAGAIKPGT PAAQYLEANG
     VERRQFNSYG SRRGNHEVMI RGTFANIRLR NQLLTDVEGG YTFNFLTGEQ SFIYDAAQDY
     QRAGIPLVVL GGKEYGSGSS RDWAAKGTAL LGVRAVIAES FERIHRSNLI GMGVLPLQYP
     SGDTAETLGL DGTEVFDITG ITELNDGVTP QTVAVTATKP DGTSVSFDAV VRIDTPGEAD
     YYRNGGILQY VLRSLVS
//
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