ID A0A1X7JMZ9_9CORY Unreviewed; 928 AA.
AC A0A1X7JMZ9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.99 {ECO:0000256|ARBA:ARBA00013250};
DE AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000256|ARBA:ARBA00031613};
DE AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000256|ARBA:ARBA00030846};
DE AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE AltName: Full=Probable 2-methyl-cis-aconitate hydratase {ECO:0000256|ARBA:ARBA00033025};
DE AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN ORFNames=SAMN06295981_1733 {ECO:0000313|EMBL:SMG28804.1};
OS Corynebacterium pollutisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1610489 {ECO:0000313|EMBL:SMG28804.1, ECO:0000313|Proteomes:UP000193309};
RN [1] {ECO:0000313|EMBL:SMG28804.1, ECO:0000313|Proteomes:UP000193309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VDS {ECO:0000313|EMBL:SMG28804.1,
RC ECO:0000313|Proteomes:UP000193309};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC Evidence={ECO:0000256|ARBA:ARBA00000118};
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 -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000256|ARBA:ARBA00005026}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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DR EMBL; FXAR01000005; SMG28804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7JMZ9; -.
DR STRING; 1610489.SAMN06295981_1733; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000193309; Unassembled WGS sequence.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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 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.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 69..603
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 733..860
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 400..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 928 AA; 100824 MW; 825B7B14BD1F80A7 CRC64;
MDSFSTRDTL TVGDVDYEIH RLDRVDTTSR LPYSLKVLLE NLLRTEDGRL VTREQIDALR
KWRPDSAAEE EIQFSPARVL MQDFTGVPCV VDLVAMRDAM TDLGGDPKKI NPLIPGELVI
DHSVIADAFG RPDALDINNQ LEFERNEERY QLLRWAQESF SDFVVVPPDT GICHQVNLEY
LSRVVFTRER DGVTQAYPDT LVGTDSHTPM VNGLGVLGWG VGGIEAEAAM LGQPASLIIP
EVVGLKLTGE LPAGTTATDL VLTVTELLRE TRVVGKFVEF FGPGVANIPL ANRATLGNMS
PEYGATVAIF PVDDVTLDYL RLTGREEQQI ALVEEYAKIQ GLWHDPDAPA EYSEVVELDL
ATVTPSIAGP KRPQDRIDLS DAPATVLGLL ADEHSIYEPA EGGVDDASAD SFPASDPVSL
TPSDQRRDAP PRRLSREQLT ANAQLGWPSD PVDVVINDTP AILDHGDVVI AAITSCTNTS
NPSVMLGAAL LAKKAVERGM RTRPWVKTTL APGSRVVTDY YDRAGLTEYM EALGFHNVGY
GCTTCIGNSG PLIPEVSEAV TDRNLNVASV LSGNRNFEGR IHPDVKMNFL ASPPLVIAYA
LAGSLHTDLL SEPLGEDADG NDVFLRDIWP TEEEIREVVE DNVRAEMFTD GYADVFEGDA
NWQGMDVPAG DKYDWTPDST YIRRPPYFDG MEVEPSPVED IEGARVLALL GDSVTTDHIS
PAGTISPASP AGRWLQEQGV APEDFNSYGS RRGNHDVMVR GTFANVRLRN QLAPGTEGGV
TRHLPDGEEM SIYDAAVRYR EEGVPLVVVA GAEYGSGSSR DWAAKGTSLL GVRAVIAESY
ERIHRSNLVG MGVLPLQFPE GESAESLGLT GEEEFSVTGL AGSEELPATV TVRAGDAEFE
AVVRVDTPAE EAYYRHGGIL PYVLRQLL
//
