ID A0A1I6ST00_9PSEU Unreviewed; 932 AA.
AC A0A1I6ST00;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05660874_03390 {ECO:0000313|EMBL:SFS80036.1};
OS Saccharopolyspora flava.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=95161 {ECO:0000313|EMBL:SFS80036.1, ECO:0000313|Proteomes:UP000198852};
RN [1] {ECO:0000313|EMBL:SFS80036.1, ECO:0000313|Proteomes:UP000198852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44771 {ECO:0000313|EMBL:SFS80036.1,
RC ECO:0000313|Proteomes:UP000198852};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOZX01000005; SFS80036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6ST00; -.
DR STRING; 95161.SAMN05660874_03390; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000198852; 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; 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 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 68..596
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 726..855
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 383..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 100913 MW; CBC743F8124BC916 CRC64;
MTAPASKDSF GARGTLNVGD ASYEVFRLSA VEGAQRLPYS LKILLENLLR TEDGANITAD
HVRALAGWDS KAEPSTEIQF TPARVIMQDF TGVPCVVDLA TMREAVAALG GDTSKVNPLA
PAEMVIDHSV IIDVFGKPDA FERNVEFEYG RNKERYQFLR WGQGAFDEFK VVPPGTGIVH
QVNIEHLARS IMSRNGQAYP DSCVGTDSHT TMVNGLGVLG WGVGGIEAEA AMLGQPVSML
IPRVVGFKLT GEIPAGATAT DVVLTITEML RKHGVVGKFV EFYGSGVASV PLANRATIGN
MSPEFGSTAA IFPIDDETVR YLKLTGRPDE QVALVEAYAK EQGLWHDPDH EPEYSEYLEL
DLSTVVPSIA GPKRPQDRIE LAQAKPSFRS SLGDYTQPPT DDAALDEAGE ESFPASDPAS
ISPHAKPELV SAANGSNGRV SRPTKVSSQE LGEFELDHGA VVIASITSCT NTSNPSVMLG
AALLARNAVD KGLTRKPWVK TSMAPGSQVV TDYYEKAGLW PYLEKLGFHL VGYGCTTCIG
NSGPLPEEIS AAVQENDLTV TSVLSGNRNF EGRINPDVKM NYLASPPLVI AYALAGTMDF
DFENDPLGND TDGNPVYLRD IWPSPQEVQQ TIDSAITNEM FTSSYEDVFK GDERWRSLPT
PEGETFEWDP QSTYVRKPPY FEGMQMEPAP VTDISGARVL ALLGDSVTTD HISPAGAIKP
DSPAGQYLSE HGIDRKDFNS YGSRRGNHEV MIRGTFANIR LRNLLLDDVQ GGYTRDFTQE
GAPQAFIYDA AQNYAAQDIP LVVLGGKEYG SGSSRDWAAK GTRLLGVRAV IAESFERIHR
SNLIGMGVIP LQFPEGSSAK SLGLDGTETY DFSGITKLND GETPETVQVT ATKADGSKVE
FDAKVRIDTP GEADYYRNGG ILQYVLRKMI RS
//
