ACNA_STRMU
ID ACNA_STRMU Reviewed; 888 AA.
AC Q59938;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Aconitate hydratase A {ECO:0000250|UniProtKB:Q8ZP52};
DE Short=ACN {ECO:0000250|UniProtKB:Q8ZP52};
DE Short=Aconitase {ECO:0000250|UniProtKB:Q8ZP52};
DE EC=4.2.1.3 {ECO:0000250|UniProtKB:Q8ZP52};
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:P09339};
DE Short=IRP-like {ECO:0000250|UniProtKB:P09339};
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:P09339};
GN Name=acn; Synonyms=citB; OrderedLocusNames=SMU_670;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 626-888.
RC STRAIN=JH1005;
RX PubMed=9006016; DOI=10.1128/jb.179.3.650-655.1997;
RA Cvitkovitch D.G., Gutierrez J.A., Bleiweis A.S.;
RT "Role of the citrate pathway in glutamate biosynthesis by Streptococcus
RT mutans.";
RL J. Bacteriol. 179:650-655(1997).
CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the tricarboxylic acid (TCA)(acetyl degradation route) and probably
CC the 2-methylcitrate cycle I (propionate degradation route). Catalyzes
CC the reversible isomerization of citrate to isocitrate via cis-
CC aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to
CC yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a
CC RNA-binding regulatory protein. {ECO:0000250|UniProtKB:P09339,
CC 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:Q8ZP52};
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:Q8ZP52}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000250|UniProtKB:Q8ZP52}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P09339}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; AE014133; AAN58404.1; -; Genomic_DNA.
DR EMBL; U62799; AAC44824.1; -; Genomic_DNA.
DR RefSeq; NP_721098.1; NC_004350.2.
DR RefSeq; WP_002261871.1; NC_004350.2.
DR AlphaFoldDB; Q59938; -.
DR SMR; Q59938; -.
DR STRING; 210007.SMU_670; -.
DR PRIDE; Q59938; -.
DR EnsemblBacteria; AAN58404; AAN58404; SMU_670.
DR KEGG; smu:SMU_670; -.
DR PATRIC; fig|210007.7.peg.595; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_9; -.
DR OMA; NGGIMQY; -.
DR PhylomeDB; Q59938; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000002512; 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:0019679; P:propionate metabolic process, methylcitrate cycle; ISS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB.
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 TIGRFAMs; TIGR01341; aconitase_1; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome;
KW RNA-binding; Tricarboxylic acid cycle.
FT CHAIN 1..888
FT /note="Aconitate hydratase A"
FT /id="PRO_0000076674"
FT BINDING 433
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 499
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 502
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 888 AA; 98054 MW; 87D3F8D315DC5BBE CRC64;
MINYTSTFTL NRQKYHYIDL VKASKDYDIE LDSLPYTIKI LLESLLRKHD DICVTKNNIE
TLFHYNSKAP QGEVPFKPSR VILQDFTGVP VVVDLASMRD AVVENGGSPD LINPEIPVDL
VIDHSVQVDF FGNQDAFDAN IDLEFERNNE RYEFLKWAEK TFENYRAVPP ATGIIHQVNL
EFLSDVIINK DGFLYPDSMF GTDSHTTMIN GIGVLGWGVG GIEAEAAMLG EASYFPIPEV
IGVRLYGELP KVATATDLAL KVTQKLRLEN VVGKFVEFFG PGLAGLSLAD RATVANMAPE
YGATCGYFPI DDETLNYMKL TNRSAEHIAL TKEYAKRNHL YHDMTNLPSY TKIVEIDLSA
IKPSISGPKR PQDLIELGQA KEEFQASLVR QFGVRGFGLG ADELAKKATV HFDDGQELEV
KTGHVAIAAI TSCTNTSNPY VLLSAGLLAK KAVERGLSVA KTVKTSLAPG SKVVTAYLRK
SGLQPYLDKL GFNLVGYGCT TCIGNSGDLV PEVAKAVQEK DLLVSAVLSG NRNFEGRVNP
LVKANFLASP PLVVAYALAG TTNIDLTSKP LGYDKNGQAV YLEDIMPAKE EVLSYIEQFV
TAELFEEEYG HVFSDSQKWN QIETENSKNY QWNQVSTYIQ NPPYFENLTN TENKIDLSAL
KVLAKFGDSV TTDHISPAGN IARNSPAARY LEENGVTYAE FNSYGSRRGN HEVMMRGTFA
NIRIKNELAD GKIGGYTKYE GEILPIYEAA MNYKKNGVST IVIAGKDYGM GSSRDWAAKG
ANLLGVKVVL AESFERIHRS NLVMMGILPL QFLDGQTAES LQLTGYETYT VELPEQPQVH
DIVKVKATSK EGTKEFQVLL RFDADADIRY YQNGGILPMV VRKKLNGG
