ID A0A0M2LID9_9SPHN Unreviewed; 878 AA.
AC A0A0M2LID9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN ORFNames=XM50_13360 {ECO:0000313|EMBL:KKI17325.1};
OS Sphingomonas sp. Ag1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1642949 {ECO:0000313|EMBL:KKI17325.1, ECO:0000313|Proteomes:UP000033997};
RN [1] {ECO:0000313|EMBL:KKI17325.1, ECO:0000313|Proteomes:UP000033997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI17325.1,
RC ECO:0000313|Proteomes:UP000033997};
RA Pei D., Yu W., Kukutla P., Xu J.;
RT "Draft Genome Sequences of Sphingomonas sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKI17325.1}.
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DR EMBL; LAZX01000094; KKI17325.1; -; Genomic_DNA.
DR RefSeq; WP_046410183.1; NZ_LAZX01000094.1.
DR AlphaFoldDB; A0A0M2LID9; -.
DR STRING; 1642949.XM50_13360; -.
DR PATRIC; fig|1642949.3.peg.363; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000033997; Unassembled WGS sequence.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
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; IPR012708; 2Me_IsoCit_deHydtase_FeS-dep.
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; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR02333; 2met_isocit_dHY; 1.
DR PANTHER; PTHR11670:SF43; 2-METHYLCITRATE DEHYDRATASE (2-METHYL-TRANS-ACONITATE FORMING); 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 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.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 67..542
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 670..800
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 878 AA; 95985 MW; B5626E1F924000FB CRC64;
MNKAFRKQLP GTPPGTSVDF FDTREAIEAI RPGAYDGLPY VSRVLAEQLV RRCDPALLTD
ALTQIVERKR DLDFPWYPAR VVCHDILGQT ALVDLAGLRD AIADKGGDPA KVNPVVPTQL
IVDHSLAVEH GGFDPQAFEK NRAIEDRRNE DRFHFIEWTK EAFQNVDVIP AGNGIMHQIN
LEKMSPVIQL RDGVAFPDTC VGTDSHTPHV DALGVIAIGV GGLEAETVML GRASMMRLPD
IVGVKLTGKR QPGITATDIV LAITEFLRKE RVVGAWLEFF GDGAESLTIG DRATISNMCP
EYGATASMFY IDQQTIDYLL LTGREPEQVK LVETYAKHTG LWADALKTAQ YERVLEFDLS
TVVRNLAGPS NPHRRLPTSA LEESGIAVGL EAAQEEERQG LLPDGAVIIA AITSCTNTSN
PRNVVAAGLV AKKANDLGLV RKPWVKTSFA PGSIVARLYL EEAGLLPELE KLGFGIVGFA
CTTCNGMSGA LDPKIQQEII DRDLYATAVL SGNRNFDGRI HPYAKQAFLA SPPLVVAYAL
AGTVRFDIEQ DVLGVVDGKE IRLKDLWPTD EEIDAIVSAH VKPEQFRKVY EPMFGARARS
AEKISPLYDW RPMSTYIRRP PYWDTEGVGA LAAHPRTLKG MRPLAILPDN ITTDHLSPSN
AILPSSAAGE YLAKMGVPEE DFNSYATHRG DHLTAMRATF ANPQLVNEMA VVDGQVKRGS
LARVEPDGVV MRMWEAMETY HQRKQPLIII AGADYGQGSS RDWAAKGVRL AGVEAIVAEG
FERIHRTNLI GMGVLPCEFK PGTTRLTLGL DGTETYDVVG ERRPGAELTL VIHRKNGETI
EVPVTCRLDT AEEVSIYEAG GVLQRFAQDF LASEAEAA
//
