ID K2GCI8_9BACI Unreviewed; 902 AA.
AC K2GCI8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=MJ3_02082 {ECO:0000313|EMBL:EKE32708.1};
OS Salimicrobium jeotgali.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX NCBI_TaxID=1230341 {ECO:0000313|EMBL:EKE32708.1, ECO:0000313|Proteomes:UP000011746};
RN [1] {ECO:0000313|EMBL:EKE32708.1, ECO:0000313|Proteomes:UP000011746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:EKE32708.1,
RC ECO:0000313|Proteomes:UP000011746};
RX PubMed=23144427; DOI=10.1128/JB.01808-12;
RA Lee S.H., Jung J.Y., Jeon C.O.;
RT "Draft Genome Sequence of Salimicrobium sp. Strain MJ3, Isolated from
RT Myulchi-Jeot, Korean Fermented Seafood.";
RL J. Bacteriol. 194:6695-6695(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 -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:EKE32708.1}.
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DR EMBL; AMPQ01000002; EKE32708.1; -; Genomic_DNA.
DR RefSeq; WP_008587723.1; NZ_JAFBFF010000002.1.
DR AlphaFoldDB; K2GCI8; -.
DR STRING; 1230341.AAV35_006655; -.
DR KEGG; sje:AAV35_006655; -.
DR PATRIC; fig|1230341.3.peg.430; -.
DR eggNOG; COG1048; Bacteria.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000011746; 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|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:EKE32708.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011746};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 74..571
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 701..828
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 902 AA; 99736 MW; C0745183938732FC CRC64;
MADHPFNAKK QFESNGKTYN YYDLKSLEDA GIGKISRLPF SIRILLESLL RQHDGRVIAD
EHVESLAKWG QSDSKQEDVP FKPSRVILQD FTGVPAVVDL ASLRKAMVDM GGKPEEINPE
VPVDLVIDHS VQVDQYGTST ALQANMELEF ERNQERYEFL HWAQKAFDNY RAVPPATGIV
HQVNLEYIAN VVHATENADG SVDTYPDTLV GTDSHTTMIN GLGVLGWGVG GIEAEAGMLG
QPSYFPAPEV IGVKLQGSFP QGTTATDLAL KVTQRLREAN VVGKFVEFFG PGLQEMPLAD
RATISNMAPE YGATCGFFPV DGESLDYMRL TGRTEEQIDL VEKYCKENNL WYDPSLEDPE
FTQLIEINLE ELEPNLSGPK RPQDLIPLSE MKESFNNSIT APEGNQGFGL DKSEFNKKAT
VEFTNGETAE MKTGALAIAA ITSCTNTSNP HVMLGAGLVA KKAVDKGLEV PEYVKTSLAP
GSKVVTRYLE DSGLMNYLNQ LGFNLVGYGC TTCIGNSGPL LPEIEQAIAD EDLTVSSVLS
GNRNFEGRIH PLVKANYLAS PPLVVAYALA GTVDIDLKNE PIGKDQQGND IYFDDIWPSQ
EEIKEQISSV VTPEIFRKEY ENVFNSNEKW NEIETTDEPL YDWDEDSTYI QNPPFFEGLS
KDFNPVKPLN GMRVIGKFGD SVTTDHISPA GAIASSMPAG EYLQEKGVSP RNFNSYGSRR
GNHEVMMRGT FANIRIRNQL AQGTEGGYTT YWPTEEVMPI YTAAMKYKED NTPLAVIAGD
DYGMGSSRDW AAKGTDLLGI ETVIAQSFER IHRSNLVMMG VLPLQFQEGE TIESLGLTGR
ETIDVEIGED VKPHDLVKVT ATDEDGNKKE FEVIARFDSD VEIDYYRHGG ILQMVLRNKL
KK
//
