ID A0A1Y0KSI8_9PSED Unreviewed; 914 AA.
AC A0A1Y0KSI8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=B9K09_12130 {ECO:0000313|EMBL:ARU88666.1};
OS Pseudomonas sp. M30-35.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1981174 {ECO:0000313|EMBL:ARU88666.1, ECO:0000313|Proteomes:UP000196445};
RN [1] {ECO:0000313|EMBL:ARU88666.1, ECO:0000313|Proteomes:UP000196445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M30-35 {ECO:0000313|EMBL:ARU88666.1,
RC ECO:0000313|Proteomes:UP000196445};
RA He A., Zhao Q., Li H., Zhang J.;
RT "Complete genome sequence of the plant growth-promoting rhizobacterium
RT Pseudomonas rhizovicinus strain M30-35.";
RL Submitted (APR-2017) 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; CP020892; ARU88666.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0KSI8; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000196445; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000196445}.
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 914 AA; 99552 MW; B842AA1811486D27 CRC64;
MPSLNSLNSR QTLKVGDKTY QYFSLPEAAK SLGNIDKLPM SLKVLLENLL RWEDDKTVTG
DDLKAIAAWL KKRSSDREIQ YRPARVLMQD FTGVPAVVDL AAMRDAMSKA GGDPQKINPL
SPVDLVIDHS VMVDKFGTNS AFTQNVDIEM QRNGERYEFL RWGQHAFDNF SVVPPGTGIC
HQVNLEYLGR TVWTKEEDGQ TFAFPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ
PVSMLIPEVI GFKLTGKLKE GITATDLVLT VTQMLRSKGV VGKFVEFYGD GLAELPLADR
ATIANMAPEY GATCGFFPVD EITLGYLRLS GRPDETVALV EAYSKAQGLW REQGQEPTFT
DSLSLDMGGV EASLAGPKRP QDRVALTQVH KAFDDFVGLQ LKPNGKEEGR LLSEGGGGTA
VGSEHSIGEI DYEFDGQSHR LKNGAVVIAA ITSCTNTSNP SVMMAAGLVA KKAVEKGLQR
KPWVKSSLAP GSKVVTEYFN AAGLTQYLDK LGFDLVGYGC TTCIGNSGPL PEPIEKAIQS
ADLTVASVLS GNRNFEGRVH PLVKTNWLAS PPLVVAYALA GNVRINIAEE SLGDDKDGNP
VYLKDIWPSQ KEISDAILKV DTAMFRKEYA EVFSGDEQWQ AIKVSEDDTY NWQSDSTYIQ
HPPFFESIAD APPHIGDISN ARVLALLGDS VTTDHISPAG NIKSDSPAGR YLREKGVEPV
DFNSYGSRRG NHEVMMRGTF ANIRIRNEML DGSEGGNTLH IPSGEQLSIY DAAMRYQQEG
TPLVVIAGKE YGTGSSRDWA AKGTNLLGVK AVLAESFERI HRSNLVGMGV LPLQFKDGQD
RKSLQLTGKE TLKITGLDGV EIRPMMNLIV EISREDGSSE RVEVLCRIDT LNEVEYFKAG
GILHYVLRQL IAGK
//
