ACND_SHEON
ID ACND_SHEON Reviewed; 867 AA.
AC Q8EJW3;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=2-methylcitrate dehydratase (2-methyl-trans-aconitate forming) {ECO:0000303|PubMed:14702315};
DE EC=4.2.1.117 {ECO:0000269|PubMed:14702315};
DE AltName: Full=Aconitate hydratase {ECO:0000303|PubMed:14702315};
DE Short=ACN {ECO:0000303|PubMed:14702315};
DE Short=Aconitase {ECO:0000303|PubMed:14702315};
DE EC=4.2.1.3 {ECO:0000269|PubMed:14702315};
GN Name=acnD; OrderedLocusNames=SO_0343;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=14702315; DOI=10.1128/jb.186.2.454-462.2004;
RA Grimek T.L., Escalante-Semerena J.C.;
RT "The acnD genes of Shewenella oneidensis and Vibrio cholerae encode a new
RT Fe/S-dependent 2-methylcitrate dehydratase enzyme that requires prpF
RT function in vivo.";
RL J. Bacteriol. 186:454-462(2004).
CC -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC via the 2-methylcitrate cycle II (propionate degradation route). In
CC vivo under anaerobic conditions, AcnD catalyzes the stereospecific
CC dehydration of (2S,3S)-methylcitrate (2-MC) to yield the trans isomer
CC of 2-methyl-aconitate (2-MCA). AcnD can also accept citrate and cis-
CC aconitate, but with a lower efficiency. 2-methylisocitrate and
CC isocitrate are not substrates. {ECO:0000269|PubMed:14702315}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3S)-2-methylcitrate = 2-methyl-trans-aconitate + H2O;
CC Xref=Rhea:RHEA:26522, ChEBI:CHEBI:15377, ChEBI:CHEBI:58853,
CC ChEBI:CHEBI:58915; EC=4.2.1.117;
CC Evidence={ECO:0000269|PubMed:14702315};
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:0000269|PubMed:14702315};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:14702315};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P09339};
CC -!- ACTIVITY REGULATION: Inhibited by ferricyanide and EDTA.
CC {ECO:0000269|PubMed:14702315}.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305|PubMed:14702315}.
CC -!- MISCELLANEOUS: Together with PrpF, able to restore the growth of prpD
CC mutant on propionate. {ECO:0000269|PubMed:14702315}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; AE014299; AAN53428.1; -; Genomic_DNA.
DR RefSeq; NP_715983.1; NC_004347.2.
DR RefSeq; WP_011070708.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EJW3; -.
DR SMR; Q8EJW3; -.
DR STRING; 211586.SO_0343; -.
DR PaxDb; Q8EJW3; -.
DR KEGG; son:SO_0343; -.
DR PATRIC; fig|211586.12.peg.333; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_6; -.
DR OMA; GRASYMR; -.
DR OrthoDB; 363064at2; -.
DR PhylomeDB; Q8EJW3; -.
DR BioCyc; SONE211586:G1GMP-328-MON; -.
DR BRENDA; 4.2.1.117; 5706.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0003994; F:aconitate hydratase activity; IBA:GO_Central.
DR GO; GO:0047780; F:citrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
DR GO; GO:0030350; F:iron-responsive element binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006101; P:citrate metabolic process; IBA:GO_Central.
DR GO; GO:0019629; P:propionate catabolic process, 2-methylcitrate cycle; IDA:UniProtKB.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR InterPro; IPR012708; 2Me_IsoCit_deHydtase_FeS-dep.
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; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR PANTHER; PTHR11670; PTHR11670; 1.
DR PANTHER; PTHR11670:SF43; PTHR11670:SF43; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR02333; 2met_isocit_dHY; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome.
FT CHAIN 1..867
FT /note="2-methylcitrate dehydratase (2-methyl-trans-
FT aconitate forming)"
FT /id="PRO_0000432942"
FT BINDING 410
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 476
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
FT BINDING 479
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P36683"
SQ SEQUENCE 867 AA; 94596 MW; DA7DBA64A0864A1F CRC64;
MSTVMNTQYR KPLPGTALDY FDTREAIEAI APGAYAKLPY TSRVLAENLV RRCEPEMLTA
SLKQIIESKQ ELDFPWFPAR VVCHDILGQT ALVDLAGLRD AIAAKGGDPA QVNPVVPTQL
IVDHSLAVEY GGFDKDAFAK NRAIEDRRNE DRFHFINWTQ KAFKNIDVIP QGNGIMHQIN
LERMSPVIHA RNGVAFPDTL VGTDSHTPHV DALGVIAIGV GGLEAESVML GRASYMRLPD
IIGVELTGKP QPGITATDIV LALTEFLRAQ KVVSSYLEFF GEGAEALTLG DRATISNMTP
EFGATAAMFY IDQQTLDYLT LTGREAEQVK LVETYAKTAG LWSDDLKQAV YPRTLHFDLS
SVVRTIAGPS NPHARVPTSE LAARGISGEV ENEPGLMPDG AVIIAAITSC TNTSNPRNVI
AAGLLARNAN AKGLTRKPWV KTSLAPGSKA VQLYLEEANL LPELESLGFG IVGFACTTCN
GMSGALDPVI QQEVIDRDLY ATAVLSGNRN FDGRIHPYAK QAFLASPPLV VAYAIAGTIR
FDIEKDVLGL DKDGKPVRLI NIWPSDAEID AVIAASVKPE QFRKVYEPMF DLSVDYGDKV
SPLYDWRPQS TYIRRPPYWE GALAGERTLK GMRPLAVLGD NITTDHLSPS NAIMMDSAAG
EYLHKMGLPE EDFNSYATHR GDHLTAQRAT FANPKLKNEM AIVDGKVKQG SLARIEPEGI
VTRMWEAIET YMDRKQPLII IAGADYGQGS SRDWAAKGVR LAGVEAIVAE GFERIHRTNL
VGMGVLPLEF KAGENRATYG IDGTEVFDVI GSIAPRADLT VIITRKNGER VEVPVTCRLD
TAEEVSIYEA GGVLQRFAQD FLESNLK
