ID K0UZ04_MYCFO Unreviewed; 923 AA.
AC K0UZ04;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=MFORT_20690 {ECO:0000313|EMBL:EJZ10340.1};
OS Mycolicibacterium fortuitum subsp. fortuitum DSM 46621 = ATCC 6841 = JCM
OS 6387.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1214102 {ECO:0000313|EMBL:EJZ10340.1, ECO:0000313|Proteomes:UP000006043};
RN [1] {ECO:0000313|EMBL:EJZ10340.1, ECO:0000313|Proteomes:UP000006043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM46621 {ECO:0000313|Proteomes:UP000006043};
RX PubMed=23105073; DOI=10.1128/JB.01461-12;
RA Ho Y.S., Adroub S.A., Aleisa F., Mahmood H., Othoum G., Rashid F.,
RA Zaher M., Ali S., Bitter W., Pain A., Abdallah A.M.;
RT "Complete Genome Sequence of Mycobacterium fortuitum subsp. fortuitum Type
RT Strain DSM46621.";
RL J. Bacteriol. 194:6337-6338(2012).
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}.
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:EJZ10340.1}.
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DR EMBL; ALQB01000095; EJZ10340.1; -; Genomic_DNA.
DR AlphaFoldDB; K0UZ04; -.
DR PATRIC; fig|1214102.3.peg.4093; -.
DR HOGENOM; CLU_013476_2_1_11; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000006043; 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.
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 60..586
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 715..845
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 923 AA; 100283 MW; 284C9EED6D46D2B7 CRC64;
MTVGDQNYEI YRLDAVPGTE KLPYSLKVLA ENLLRTEDGA NITKDHIEAI ANWDPSAEPS
VEIQFTPARV LMQDFTGVPC IVDLATMREA VAALGGDPDK VNPLSPAEMV IDHSVILDVF
GNAGAFERNV ELEYERNSER YQFLRWGQGA FDDFKVVPPG TGIVHQVNIE YLARVVMTRN
GVAYPDTCVG TDSHTTMENG LGVLGWGVGG IEAEAAMLGQ PVSMLIPRVV GFKLTGEIKP
GVTATDVVLT VTDMLRKHGV VGKFVEFYGK GVAEVPLANR ATLGNMSPEF GSTAAIFPID
DETINYLRLT GRTEEQLALV EAYAKTQGMW HNPDREPVFS EYLELDLSTV VPSISGPKRP
QDRIELSDAK NAFRKDIHNY VEENLPVEHT QLDEAIEESF PASDPAKLTF ADDGAVDVRP
SAANGAEGRP TKPITVRSDE RGEFVLDHGA VVVAGITSCT NTSNPSVMIG AALLAKKAVE
KGLTSKPWVK TNMAPGSQVV TDYYNKAGLW PYLEKLGYYL GGYGCTTCIG NTGPLPDEIS
KAINDNDLSV TAVLSGNRNF EGRISPDVKM NYLASPPLVI AYGIAGTMDF DFETDPLGQD
QEGNDVFLKD IWPSAKEIEE TIASSINREM FTDSYADVFK GDDRWRSLST PEGNIFEWDD
ASTYVRKAPY FDGMPAEPEP VVDIKGARVL ALLGDSVTTD HISPAGSIKP GTPAAQYLDA
NGVERKDYNS LGSRRGNHEV MIRGTFANIR LRNQLLDDVS GGYTRDFTQP GGPQSFIYDA
SVNYKEAGIP LVVLGGKEYG SGSSRDWAAK GTVLLGVKAV ITESFERIHR SNLIGMGVIP
LQFPAGESAA SLKLDGTETY DITGIEALNE GKTPKTVKVT ATKEDGSKVE FDAVVRIDTP
GEADYYRNGG ILQYVLRNML KSK
//
