ACNA_MYCS2
ID ACNA_MYCS2 Reviewed; 943 AA.
AC A0QX20; A4ZHS6; I7G8K0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Aconitate hydratase A {ECO:0000250|UniProtKB:O53166};
DE Short=ACN {ECO:0000250|UniProtKB:O53166};
DE Short=Aconitase {ECO:0000250|UniProtKB:O53166};
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:O53166};
DE AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE AltName: Full=Iron-responsive protein-like {ECO:0000250|UniProtKB:O53166};
DE Short=IRP-like {ECO:0000250|UniProtKB:O53166};
DE AltName: Full=Probable 2-methyl-cis-aconitate hydratase {ECO:0000250|UniProtKB:Q8ZP52};
DE EC=4.2.1.99 {ECO:0000250|UniProtKB:Q8ZP52};
DE AltName: Full=RNA-binding protein {ECO:0000250|UniProtKB:O53166};
GN Name=acnA; Synonyms=acn; OrderedLocusNames=MSMEG_3143, MSMEI_3062;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP PUPYLATION AT LYS-394, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20094657; DOI=10.1039/b916104j;
RA Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA Barry C.E. III, Bark S., Dorrestein P.C.;
RT "Expansion of the mycobacterial 'PUPylome'.";
RL Mol. Biosyst. 6:376-385(2010).
CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the tricarboxylic acid (TCA)(acetyl degradation route) and probably
CC via the 2-methylcitrate cycle I (propionate degradation route).
CC Catalyzes the reversible isomerization of citrate to isocitrate via
CC cis-aconitate. The apo form of AcnA functions as a RNA-binding
CC regulatory protein. Could catalyze the hydration of 2-methyl-cis-
CC aconitate to yield (2R,3S)-2-methylisocitrate.
CC {ECO:0000250|UniProtKB:O53166, ECO:0000250|UniProtKB:Q8ZP52}.
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:0000250|UniProtKB:O53166};
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:0000250|UniProtKB:Q8ZP52};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P09339};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P09339};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000250|UniProtKB:O53166}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000250|UniProtKB:O53166}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O53166}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; DQ866855; ABJ96316.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK73859.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39526.1; -; Genomic_DNA.
DR RefSeq; WP_011728843.1; NZ_SIJM01000002.1.
DR RefSeq; YP_887458.1; NC_008596.1.
DR AlphaFoldDB; A0QX20; -.
DR SMR; A0QX20; -.
DR STRING; 246196.MSMEI_3062; -.
DR PRIDE; A0QX20; -.
DR EnsemblBacteria; ABK73859; ABK73859; MSMEG_3143.
DR EnsemblBacteria; AFP39526; AFP39526; MSMEI_3062.
DR GeneID; 66734544; -.
DR KEGG; msg:MSMEI_3062; -.
DR KEGG; msm:MSMEG_3143; -.
DR PATRIC; fig|246196.19.peg.3103; -.
DR eggNOG; COG1048; Bacteria.
DR OMA; NGGIMQY; -.
DR OrthoDB; 363064at2; -.
DR SABIO-RK; A0QX20; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR GO; GO:0003994; F:aconitate hydratase activity; ISS:UniProtKB.
DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
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; PTHR11670; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 1: Evidence at protein level;
KW Iron; Iron-sulfur; Isopeptide bond; Lyase; Metal-binding;
KW Reference proteome; RNA-binding; Tricarboxylic acid cycle; Ubl conjugation.
FT CHAIN 1..943
FT /note="Aconitate hydratase A"
FT /id="PRO_0000396818"
FT REGION 422..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 544
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 547
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT CROSSLNK 394
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20094657"
SQ SEQUENCE 943 AA; 102171 MW; BD10F939FA09F201 CRC64;
MSSENTGKSS LNSFGARDTL TVGDQSYEIY RLNAVPGTEK LPYSLKVLAE NLLRTEDGAN
ITKDHIEAIA NWDPNAEPSI EIQFTPARVI MQDFTGVPCI VDLATMREAV AALGGDPNKV
NPLAPAELVI DHSVILDVFG NASAFERNVE LEYERNAERY QFLRWGQGAF DDFKVVPPGT
GIVHQVNIEY LARTVMVRDG VAYPDTCVGT DSHTTMVNGL GVLGWGVGGI EAEAAMLGQP
VSMLIPRVVG FKLSGEIKPG VTATDVVLTV TDMLRRHGVV GKFVEFYGKG VAEVPLANRA
TLGNMSPEFG STAAIFPIDE ETINYLRLTG RTDEQLALVE AYAKAQGMWH DPEREPVFSE
YLELDLSTVV PSISGPKRPQ DRIELTDAKN AFRKDIHNYV EQNHPTPETK LDEAVEESFP
ASDPVSLSFA DDGAPDMRPS AANGATGRPT NPVLVHSEER GDFVLDHGAV VVAGITSCTN
TSNPSVMLGA ALLAKKAVEK GLTTKPWVKT NMAPGSQVVT DYYNKAGLWP YLEKLGYYLG
GYGCTTCIGN TGPLPEEISK AINDNDLAVT AVLSGNRNFE GRISPDVKMN YLASPPLVIA
YGIAGTMDFD FESDPLGQDS EGNDVFLRDI WPSAAEIEET IASSINREMF TESYADVFKG
DDRWRSLPTP EGDTFEWDPA STYVRKAPYF DGMPAEPEPV SDIKGARVLA LLGDSVTTDH
ISPAGAIKPG TPAAQYLDAN GVERKDYNSL GSRRGNHEVM IRGTFANIRL RNQLLDDVSG
GYTRDFTQPG GPQAFIYDAS ENYKKAGIPL VVLGGKEYGS GSSRDWAAKG TVLLGVKAVI
TESFERIHRS NLIGMGVIPL QFPAGESAAS LKLDGTETYD IEGIEELNSG KTPKTVHVTA
TKEDGSKVEF DAVVRIDTPG EADYYRNGGI LQYVLRNMLK SSK
