ID W5IKF0_PSEUO Unreviewed; 910 AA.
AC W5IKF0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 ORFNames=PM1_0223060 {ECO:0000313|EMBL:ETM63390.1};
OS Pseudomonas sp. (strain M1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=95619 {ECO:0000313|EMBL:ETM63390.1};
RN [1] {ECO:0000313|EMBL:ETM63390.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ETM63390.1};
RX PubMed=10388678;
RA Iurescia S., Marconi A.M., Tofani D., Gambacorta A., Paterno A.,
RA Devirgiliis C., van der Werf M.J., Zennaro E.;
RT "Identification and sequencing of beta-myrcene catabolism genes from
RT Pseudomonas sp. strain M1.";
RL Appl. Environ. Microbiol. 65:2871-2876(1999).
RN [2] {ECO:0000313|EMBL:ETM63390.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M1 {ECO:0000313|EMBL:ETM63390.1};
RA Soares-Castro P.M., Santos P.M.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ETM63390.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ETM63390.1};
RX PubMed=23405299;
RA Soares-Castro P., Santos P.M.;
RT "Towards the Description of the Genome Catalogue of Pseudomonas sp. Strain
RT M1.";
RL Genome Announc. 1:E00146-E00112(2013).
RN [4] {ECO:0000313|EMBL:ETM63390.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M1 {ECO:0000313|EMBL:ETM63390.1};
RA Soares-Castro P., Santos P.M.;
RT "Decyphering the genome repertoire of Pseudomonas sp. M1 towards myrcene
RT biotransformation.";
RL Submitted (DEC-2013) 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}.
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:ETM63390.1}.
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; ANIR02000003; ETM63390.1; -; Genomic_DNA.
DR RefSeq; WP_009622811.1; NZ_CP094343.1.
DR AlphaFoldDB; W5IKF0; -.
DR eggNOG; COG1048; Bacteria.
DR UniPathway; UPA00223; UER00718.
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..836
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 910 AA; 99239 MW; 26D0981AE360BA4D CRC64;
MPAVDSLNSL RTLEVGGKTY HYYSLPEAAK QLGDLDKLPK SLKVLLENLL RWEDNHTVNA
DDLRALAGWL KERRSDREIQ YRPARVLMQD FTGVPAVVDL AAMRDAMAKA GGDPQKINPL
SPVDLVIDHS VMVDRYASHA AFAENVEIEM QRNGERYAFL RWGQNAFDNF RVVPPGTGIC
HQVNLEYLGR TVWTRDEDGR TYAFPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ
PVSMLIPEVV GFKLTGKLKE GITATDLVLT VTQMLRQKGV VGKFVEFYGD GLADLPLADR
ATIANMAPEY GATCGFFPVD EITLGYLRLS GRPEETVKLV EAYCKAQGLW REKGHEPVFT
DALQLDMGEV EASLAGPKRP QDRVPLGQVG KAFADFLALQ PKAARSPEVS RLLNEGGGGA
AVGSAESQGV EYQHEGKSYH LQDGAVVIAA ITSCTNTSNP SVMMAAGLLA KKALEKGLQR
KPWVKSSLAP GSKVVTDYFK AAGLTQYLDE LGFDLVGYGC TTCIGNSGPL LEPIEKAIQQ
ADLTVASVLS GNRNFEGRVH PLVKTNWLAS PPLVVAYALA GSVRLDLTKD ALGTGKDGQP
VYLKDIWPSQ REIAEAIQKV DTAMFHKEYA EVFQGDEKWR AIQVPQAQTY TWQADSTYIQ
HPPFFEHIAD APPKVADIEK ARVLAVLGDS VTTDHISPAG NIKKDSPAGR YLSEHGVAYA
DFNSYGSRRG NHEVMMRGTF ANIRIKNEML GGEEGGNTLH VPSGEKLAIY DAAMRYQAEG
TPLLIIAGKE YGTGSSRDWA AKGTNLLGVK AVIAESFERI HRSNLVGMGV LPLQFTGGQD
RKALNLTGKE VLNIRGLDGE LKPHMTLKVE VTREDGQQES FEVLCRIDTL NEVEYFKAGG
ILHYVLRSLI
//
