ID K2KX37_9GAMM Unreviewed; 865 AA.
AC K2KX37;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Aconitate hydratase {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU361275};
DE Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU361275};
GN ORFNames=A10D4_02442 {ECO:0000313|EMBL:EKE87064.1};
OS Idiomarina xiamenensis 10-D-4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=740709 {ECO:0000313|EMBL:EKE87064.1, ECO:0000313|Proteomes:UP000014115};
RN [1] {ECO:0000313|EMBL:EKE87064.1, ECO:0000313|Proteomes:UP000014115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10-D-4 {ECO:0000313|EMBL:EKE87064.1,
RC ECO:0000313|Proteomes:UP000014115};
RX PubMed=23209204; DOI=10.1128/JB.01855-12;
RA Lai Q., Wang L., Wang W., Shao Z.;
RT "Genome Sequence of Idiomarina xiamenensis Type Strain 10-D-4.";
RL J. Bacteriol. 194:6938-6938(2012).
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 -!- 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:EKE87064.1}.
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DR EMBL; AMRG01000002; EKE87064.1; -; Genomic_DNA.
DR RefSeq; WP_008487510.1; NZ_AMRG01000002.1.
DR AlphaFoldDB; K2KX37; -.
DR STRING; 740709.A10D4_02442; -.
DR PATRIC; fig|740709.3.peg.493; -.
DR eggNOG; COG1048; Bacteria.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000014115; 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: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 NCBIfam; TIGR01341; aconitase_1; 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 4Fe-4S {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|RuleBase:RU361275, ECO:0000313|EMBL:EKE87064.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000014115}.
FT DOMAIN 68..535
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 659..790
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 865 AA; 94914 MW; 2CFE03D45080E363 CRC64;
MSNNQAYRKP LPGTTLSYYD TRAAVEAIKP GSYDGLPYTS RILAENLVRR CDPATLDACL
SQIIERKRDL DFPWFPARVV CHDILGQTAL VDLAGLRDAI AEKGGDPAKV NPVVPTQLIV
DHSLAVEHAG FEKDAFEKNR AIEDRRNDDR FHFINWTKTA FKNVDVIPPG NGIMHQINLE
KMSPVVQVRD GVAFPDTCVG TDSHTPMVDA LGVISVGVGG LEAETVMLGR ASYMRLPDIV
GVELSGQLQP GITGTDMVLA LTEFLRREKV VGAYLEFFGE GARKLTVGDR ATISNMTPEY
GATAAMFSID EQTIDYLKLT GRDDEQVQLV EKFAKHTGLW ADSLAQVQYE RVLRFDLSTV
RRNLAGPSNP HALLPAEQLA ERGIAAPYQQ SEGEMPDGAV IIAAITSCTN TSNPRNMVAA
GLIARNANRL GLTRKPWVKS SLAPGSKTVK MYLEEAELLP ELEQLGFGVV AFACTTCNGM
SGALDADIQQ EIIDRDLYAT AVLSGNRNFD GRIHPYAKQA FLASPPLVVA YAIAGSIRFD
IEKDVLGYDK DGNAVTLKDI WPSDEEIDAI VKKAVKPEQF RTVYDPMFSL SVDYGDDNDP
LYQWRPQSTY IRRPPYWEGA LAGERSLRGM RPLAVLGDNI TTDHLSPSNA IMADSAAGEY
LAKMGVPEQD FNSYATHRGD HLTAQRATFA NPKLLNEMVQ ENGKVKQGSL ARIEPEGQVV
RMWEAIETYM QRQQPLIIVA GADYGQGSSR DWAAKGVRLA GVQVIAAEGF ERIHRTNLIG
MGVLPLQFEA GTTRHTLAID GTESYDVEGE LAPGEQMTLL INRRDGSSQR VPMICRLDTA
EELSIYLAGG VLQRFAKDFL EAEAS
//
