ID A1SAU2_SHEAM Unreviewed; 861 AA.
AC A1SAU2;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN OrderedLocusNames=Sama_3296 {ECO:0000313|EMBL:ABM01499.1};
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297 {ECO:0000313|EMBL:ABM01499.1, ECO:0000313|Proteomes:UP000009175};
RN [1] {ECO:0000313|EMBL:ABM01499.1, ECO:0000313|Proteomes:UP000009175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B {ECO:0000313|Proteomes:UP000009175};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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DR EMBL; CP000507; ABM01499.1; -; Genomic_DNA.
DR RefSeq; WP_011761403.1; NC_008700.1.
DR AlphaFoldDB; A1SAU2; -.
DR STRING; 326297.Sama_3296; -.
DR KEGG; saz:Sama_3296; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_6; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000009175; Chromosome.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:ABM01499.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009175}.
FT DOMAIN 69..533
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 656..787
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 861 AA; 94219 MW; 47750044C49B194A CRC64;
MNTQFRKPLP GTNLSFFDTR EAVDAIAPGA FDKLPYTSKV LAENLLRKAE PARLNDFLSQ
LIFRKQDLDF PWFPARVVCH DILGQTALVD LAGLRDAIAA KGGDPAKVNP VVPTQLIVDH
SLAVEHGGFE KDAFEKNRAI EDRRNDDRFH FINWTKKAFR NVDVIPPGNG IMHQINLEKM
SPVIQVRDGI AFPDTCVGTD SHTPHVDSLG VIAIGVGGLE AENVMLGRAS WMRLPDIVGV
ELTGKPNPGI TATDVVLALT EFLRKERVVG AYLEFFGEGA KALTLGDRAT ISNMTPEYGA
TAAMFYIDEQ TIDYLRLTGR DEKQVELVEN YAKTTGLWAD AMTGADYGRI LTFDLSSVVR
NMAGPSNPHA RLATSDLAAK GIAADWQEES GKMPDGAVII AAITSCTNTS NPRNVIAAGL
IARNAVQKGL VRKPWVKTSL APGSKAVELY LKEAGLLPYL EQLGFGIVAF ACTTCNGMSG
ALDPVIQQEI IERDLYATAV LSGNRNFDGR IHPYAKQAFL ASPPLVVAYA IAGTVRFDIE
KDVLGIDDAG NAVTLKDLWP EDAEIDAIIK SSVKPEQFRA VYDPMFNLAV EYGTEKPLYD
WRPQSTYIRR PPYWEGALAG ERTLSGMRPL AVLGDNITTD HLSPSNAILA SSAAGEYLAK
MGLPEEDFNS YATHRGDHLT AQRATFANPK LFNEMVKDAD GKVKQGSLAR LEPEGKVLRM
WETIETYMER KQPLIIVAGK DYGQGSSRDW AAKGVRLAGV EVIVAEGFER IHRTNLVGMG
VLPLEFMPGE TRMTYGIDGT ETFDVKGERT PGAELTLLIR RQNGETVEVP VRCRLDTAEE
VSIYEAGGVL QRFAQDFLAN S
//
