ID Q1I7B0_PSEE4 Unreviewed; 913 AA.
AC Q1I7B0;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 111.
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:CAK16472.1};
GN OrderedLocusNames=PSEEN3756 {ECO:0000313|EMBL:CAK16472.1};
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676 {ECO:0000313|EMBL:CAK16472.1, ECO:0000313|Proteomes:UP000000658};
RN [1] {ECO:0000313|EMBL:CAK16472.1, ECO:0000313|Proteomes:UP000000658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48 {ECO:0000313|EMBL:CAK16472.1,
RC ECO:0000313|Proteomes:UP000000658};
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CT573326; CAK16472.1; -; Genomic_DNA.
DR RefSeq; WP_011534849.1; NC_008027.1.
DR AlphaFoldDB; Q1I7B0; -.
DR STRING; 384676.PSEEN3756; -.
DR GeneID; 32806795; -.
DR KEGG; pen:PSEEN3756; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_6; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000000658; 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.
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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 75..581
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 710..837
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 913 AA; 99002 MW; 6D6B60A68CD13A48 CRC64;
MPSLDSLKTL KNLDVAGHAY HYFSLAEAAN QLGDLQRLPM SLKVLLENLL RWEDGKTVTV
DDLRALAKWL AERRSDREIQ YRPARVLMQD FTGVPAVVDL AAMRAAMAKA GGDPQRINPL
SPVDLVIDHS VMVDRYASPS AFAQNVDIEM QRNGERYAFL RWGQSAFANF RVVPPGTGIC
HQVNLEYLGR TVWTNEQDGR TFAFPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ
PVSMLIPEVI GFKLTGKLRE GITATDLVLT VTQMLRKKGV VGKFVEFYGD GLADLPLADR
ATIANMAPEY GATCGFFPVD QVTLDYLRLS GRPEAAVQLV EAYCKAQGLW RLPGQEPLFT
DTLALDMHDV EASLAGPKRP QDRVALGQVS QAFDHFIELQ PKPLAKEVGR LESEGGGGVA
VGNADQAGEI DYTHGGQTHT LRDGAVVIAA ITSCTNTSNP SVMMAAGLVA KKAVEKGLQR
KPWVKSSLAP GSKVVTDYFK AAGLTPYLDQ LGFDLVGYGC TTCIGNSGPL DDAIEKAIGS
ADLTVASVLS GNRNFEGRVH PLVKTNWLAS PPLVVAYALA GSVRVDLTQD ALGTGKDGRP
VYLRDIWPSQ QEIAEAVANV DTRMFHKEYA EVFAGDAQWQ AIAVPKAATY AWQDASTYIQ
HPPFFDDIGG PPPEVRDIQS ARILALLGDS VTTDHISPAG NIKADSPAGR YLREKGVEPR
DFNSYGSRRG NHEVMMRGTF ANIRIRNEML GGEEGGNTLY VPSGEKLSIY DAAMRYQRDG
TPLVVIAGQE YGTGSSRDWA AKGTNLLGVK AVLAESFERI HRSNLVGMGV LPLQFKAGDD
RKRLGLTGRE RIDVLGLSGA QIRPGMDLPV RITREDGQTL QVEVLCRIDT LNEVEYFKSG
GILHFVLRQL IAG
//
