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Database: UniProt
Entry: A0A0G3EN87_9BURK
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ID   A0A0G3EN87_9BURK        Unreviewed;       901 AA.
AC   A0A0G3EN87;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
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:AKJ68528.1};
GN   ORFNames=ABW99_10195 {ECO:0000313|EMBL:AKJ68528.1};
OS   Pandoraea thiooxydans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Pandoraea.
OX   NCBI_TaxID=445709 {ECO:0000313|EMBL:AKJ68528.1, ECO:0000313|Proteomes:UP000036700};
RN   [1] {ECO:0000313|Proteomes:UP000036700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25325 {ECO:0000313|Proteomes:UP000036700};
RA   Lim Y.L., Ee R., Yong D., How K.Y., Yin W.F., Chan K.G.;
RL   Submitted (JUN-2015) 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   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC       {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR   EMBL; CP011568; AKJ68528.1; -; Genomic_DNA.
DR   RefSeq; WP_047214377.1; NZ_CP014839.1.
DR   AlphaFoldDB; A0A0G3EN87; -.
DR   STRING; 445709.ABW99_10195; -.
DR   KEGG; ptx:ABW99_10195; -.
DR   PATRIC; fig|445709.3.peg.2178; -.
DR   OrthoDB; 9764318at2; -.
DR   UniPathway; UPA00223; UER00718.
DR   Proteomes; UP000036700; 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:0009098; P:leucine biosynthetic process; 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|ARBA:ARBA00022485, 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:UP000036700}.
FT   DOMAIN          62..563
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          695..825
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   901 AA;  97976 MW;  960E3A14EB3ED179 CRC64;
     MAHNLHKTLK EFDIGGKKKG QFYSLPQLGK ALGVDVSRLP VSIRIVLESV LRNCDGKKVT
     EEHVKQLANW KPTANRVDEI PFVVARVVLQ DFTGVPLLAD LAAMRNVADR MGKNPKRIEP
     LVPVDLVVDH SVQIDHFREK KALDLNMKIE FQRNNERYQF MKWGMQAFDT FGVVQPGFGI
     VHQVNLEYLA RGVHKKNNVY YPDTLVGTDS HTTMINGIGV VGWGVGGIEA EAGMLGQPVY
     FLTPDVVGVE LKGRLREGVT ATDLVLTITE MLRREKVVGK FVEFFGEGTA SLALPDRATI
     GNMAPEYGAT MGFFPVDEKT IEYFEGTGRT KAEIAAFEAY FKAQKLFGIP KAGQIDYTKV
     VTLDLGTVAP SLAGPKRPQD RIEITNVKQT FTDLFSKPVA ENGFNKNPAD LAQAYTAANG
     VDLKSGDVLI AAITSCTNTS NPSVLLAAGL LAKKAVEAGL KVAPHIKTSL APGSRVVTKY
     LEAAGLLPYL EKLGFGVTAY GCTTCIGNAG DLLPEFNEAI TKNDIVAAAV LSGNRNFEAR
     IHPNIRANFL ASPPLVVAYA IAGNVTRDLM TEPVGKGKGG KDIYLGDIWP TSEEVHKLLK
     FAMNAKTFKA NYEEVKKPSP LWAKIKGSNG QVYDWPSSTY IAEPPFFEGF EMEPSDDIAP
     IKGARALGVF GDSVTTDHIS PAGSIKETSP AGKWLLENGV LKADFNSYGS RRGNHEVMMR
     GTFANVRIKN LMIPPTADGS RVEGGLTIHQ PSGEQMSIYD AAMKYVGSDT PTVIFGGEEY
     GTGSSRDWAA KGTQLLGVKA VVARSFERIH RSNLVGMGVL PLQFKGDDSV DSLGITGAET
     YDIEGLSSDL KPQQDVTLVI HRKNGETKRV SLLLRIDTPI EVDYYKHGGI LPFVLRQLLV
     A
//
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