ACEA_HALVD
ID ACEA_HALVD Reviewed; 345 AA.
AC D4GTL3; Q977U5;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:9738442};
DE Short=ICL {ECO:0000303|PubMed:9738442};
DE EC=4.1.3.1 {ECO:0000269|PubMed:9738442};
DE AltName: Full=Isocitrase {ECO:0000303|PubMed:9738442};
DE AltName: Full=Isocitratase {ECO:0000303|PubMed:9738442};
GN Name=aceA; OrderedLocusNames=HVO_1984; ORFNames=C498_05201;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18, FUNCTION, MASS
RP SPECTROMETRY, AND SUBUNIT.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=11513957; DOI=10.1016/s0167-4781(01)00263-9;
RA Serrano J.A., Bonete M.J.;
RT "Sequencing, phylogenetic and transcriptional analysis of the glyoxylate
RT bypass operon (ace) in the halophilic archaeon Haloferax volcanii.";
RL Biochim. Biophys. Acta 1520:154-162(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=9738442; DOI=10.1016/s0014-5793(98)00911-9;
RA Serrano J.A., Camacho M., Bonete M.J.;
RT "Operation of glyoxylate cycle in halophilic archaea: presence of malate
RT synthase and isocitrate lyase in Haloferax volcanii.";
RL FEBS Lett. 434:13-16(1998).
CC -!- FUNCTION: Involved in the metabolic adaptation in response to
CC environmental changes. Catalyzes the reversible formation of succinate
CC and glyoxylate from isocitrate, a key step of the glyoxylate cycle,
CC which operates as an anaplerotic route for replenishing the
CC tricarboxylic acid cycle during growth on fatty acid substrates.
CC {ECO:0000269|PubMed:11513957, ECO:0000269|PubMed:9738442}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate = glyoxylate + succinate;
CC Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:36655; EC=4.1.3.1; Evidence={ECO:0000269|PubMed:9738442};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A9G6};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.16 uM for isocitrate (at pH 7 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:9738442};
CC pH dependence:
CC Optimum pH is 7. Very little activity is detected at pH 6.1 or 8.0.
CC {ECO:0000269|PubMed:9738442};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius. Very little activity is
CC found above 65 degrees Celsius, and the activity at 40 degrees
CC Celsius is 50% of the maximum. {ECO:0000269|PubMed:9738442};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 1/2. {ECO:0000305|PubMed:9738442}.
CC -!- SUBUNIT: Homotetramer or homotrimer. {ECO:0000269|PubMed:11513957,
CC ECO:0000269|PubMed:9738442}.
CC -!- MASS SPECTROMETRY: Mass=38690; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11513957};
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC {ECO:0000305}.
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DR EMBL; AJ250922; CAC48388.1; -; Genomic_DNA.
DR EMBL; CP001956; ADE02416.1; -; Genomic_DNA.
DR EMBL; AOHU01000038; ELY34498.1; -; Genomic_DNA.
DR RefSeq; WP_004041865.1; NZ_AOHU01000038.1.
DR AlphaFoldDB; D4GTL3; -.
DR SMR; D4GTL3; -.
DR STRING; 309800.C498_05201; -.
DR EnsemblBacteria; ADE02416; ADE02416; HVO_1984.
DR EnsemblBacteria; ELY34498; ELY34498; C498_05201.
DR GeneID; 8926360; -.
DR KEGG; hvo:HVO_1984; -.
DR PATRIC; fig|309800.29.peg.1012; -.
DR eggNOG; arCOG00582; Archaea.
DR HOGENOM; CLU_027389_3_2_2; -.
DR OMA; GFPDLEM; -.
DR OrthoDB; 53531at2157; -.
DR UniPathway; UPA00703; UER00719.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0004451; F:isocitrate lyase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006097; P:glyoxylate cycle; IDA:UniProtKB.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR006254; Isocitrate_lyase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PIRSF; PIRSF001362; Isocit_lyase; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glyoxylate bypass; Lyase; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..345
FT /note="Isocitrate lyase"
FT /id="PRO_0000429585"
FT REGION 318..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 58..60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 136..137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 230..234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ SEQUENCE 345 AA; 39015 MW; 8E65DEA7EBEB7A33 CRC64;
MNPTELDSDV FAQDVDNQKA RELREMLNTQ DFVFAPGMYH ALDARLAEMT GHDAAYMSGY
STVLGQFGFP DLEMVTMTEM VENAKRMVEA TNLPVIADCD TGYGGIHNVR RAVREYEKAG
VAAVHIEDQT TPKRCGHIAG KQIVSREKAK ARFEAAVDAK QSEDTVVIAR TDAYGSSNGD
WDEHVERGRI YADAGVDIVW PEMPNPSRED AVAYAEEIHE THPDLKLAFN YSSSFAWSEE
EDPLTFQELG DLGYKYIFIT LFGLHSGAHA VYEDFKKLAE QDEEGQFDLE QRYLDHPTES
HHELSFVSRY QDIETEFDPE ARRRIEESEG FSEEQADPIT SNDDD
