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
//