ID A0A0C2I6P1_9PSED Unreviewed; 913 AA.
AC A0A0C2I6P1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=UCMB321_1214 {ECO:0000313|EMBL:KIH84886.1};
OS Pseudomonas batumici.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=226910 {ECO:0000313|EMBL:KIH84886.1, ECO:0000313|Proteomes:UP000031535};
RN [1] {ECO:0000313|EMBL:KIH84886.1, ECO:0000313|Proteomes:UP000031535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCM B-321 {ECO:0000313|EMBL:KIH84886.1,
RC ECO:0000313|Proteomes:UP000031535};
RA Klochko V.V., Zelena L.B., Elena K.A., Reva O.N.;
RT "Complete genome of Pseudomonas batumici UCM B-321 producer of the batumin
RT antibiotic with strong antistaphilococcal and potential anticancer
RT activity.";
RL Submitted (JAN-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}.
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:KIH84886.1}.
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DR EMBL; JXDG01000012; KIH84886.1; -; Genomic_DNA.
DR RefSeq; WP_040064627.1; NZ_JXDG01000012.1.
DR AlphaFoldDB; A0A0C2I6P1; -.
DR STRING; 226910.UCMB321_1214; -.
DR PATRIC; fig|226910.6.peg.1205; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000031535; Unassembled WGS sequence.
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 913 AA; 99115 MW; 927C9B204DF9C1A9 CRC64;
MSSLDSLKAL KTLDVGSKTY HYFSLPAAAK SLGHLDKLPM SLKVLLENLL RWEDGKTVTG
ADLKAIAAWL KRRSSDREIQ YRPARVLMQD FTGVPAVVDL AAMRAAVAKA GGDPQRINPL
SPVDLVIDHS VMVDKFATAQ AFGQNVDIEM QRNGERYAFL RWGQNAFDNF SVVPPGTGIC
HQVNLEYLGR TVWTKDEDGR TYAFPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ
PVSMLIPEVI GFKLTGKLKE GITATDLVLT VTQMLRTKGV VGKFVEFYGD GLAELPLADR
ATIANMAPEY GATCGFFPVD QVTLDYLRLS GRPSETVQLV EAYSKIQGLW RLPGHEPTFT
DSLALDMGSV EASLAGPKRP QDRVSLPDVA QAFSDFMALQ FKPVHKDEGR LESEGGGGVA
VGNADLVGEV DYSDEGQTYR LKNGAVVIAA ITSCTNTSNP SVMMAAGLVA KKAVEKGLKR
KPWVKSSLAP GSKVVTDYYK AAGLNRYLDE LGFALVGYGC TTCIGNSGPL PEPIEKAVTQ
SDLTVASVLS GNRNFEGRVH PLVKTNWLAS PPLVVAYALA GSVRIDISRE PLGEDRDGKP
VYLRDIWPSQ KEIADAVAQV DTAMFHKEYA EVFAGDAQWQ AIEVPQAATY VWQKDSTYIK
HPPFFDNIAG PLPVIEDIQD ARVLALLGDS VTTDHISPAG NIKADSPAGR YLRELGVEPR
DFNSYGSRRG NHEVMMRGTF ANIRIRNEML GGEEGGNTFH VPSGEKLSIY DAAMRYQAEG
TPLVVIAGQE YGTGSSRDWA AKGTNLLGVK AVIAESFERI HRSNLVGMGV LPLQFKLDQN
RKSLNLTGKE TLSIGGLSST ELQPRMNLPL TLTREDGSQE KIDVLCRIDT LNEVEYFKAG
GILHYVLRQL IAS
//
