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ACEAA_MYCTU
ID   ACEAA_MYCTU             Reviewed;         367 AA.
AC   O07718; F2GH80; I6Y7U7; L0T829;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Putative isocitrate lyase subunit A {ECO:0000305};
DE            Short=ICL {ECO:0000250|UniProtKB:Q8VJU4};
DE            EC=4.1.3.1 {ECO:0000250|UniProtKB:Q8VJU4};
DE   AltName: Full=Isocitrase {ECO:0000250|UniProtKB:Q8VJU4};
DE   AltName: Full=Isocitratase {ECO:0000250|UniProtKB:Q8VJU4};
GN   Name=aceAa; OrderedLocusNames=Rv1915, RVBD_1915, LH57_10430;
GN   ORFNames=P425_01980;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RG   The Broad Institute Genome Sequencing Platform;
RA   Galagan J., Kreiswirth B., Dobos K., Fortune S., Fitzgerald M., Young S.K.,
RA   Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Kreiswirth B., Gomez J., Victor T., Desjardins C., Abeel T.,
RA   Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., Murphy C., Naylor J., Pearson M., Poon T.W.,
RA   Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA   Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA   Monaco A., King S., Sohrabi A.;
RT   "Phylogenetic analysis of Mycobacterial species using whole genome
RT   sequences.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Together with AceAb, they could catalyze the formation of
CC       succinate and glyoxylate from isocitrate. {ECO:0000305}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q8VJU4};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P9WKK7};
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP44682.1; -; Genomic_DNA.
DR   EMBL; CP003248; AFN49847.1; -; Genomic_DNA.
DR   EMBL; JLDD01000021; KBJ34149.1; -; Genomic_DNA.
DR   EMBL; CP009480; AIR14660.1; -; Genomic_DNA.
DR   RefSeq; NP_216431.1; NC_000962.3.
DR   RefSeq; WP_003906697.1; NZ_NVQJ01000034.1.
DR   AlphaFoldDB; O07718; -.
DR   SMR; O07718; -.
DR   STRING; 83332.Rv1915; -.
DR   PaxDb; O07718; -.
DR   PRIDE; O07718; -.
DR   DNASU; 885639; -.
DR   GeneID; 885639; -.
DR   KEGG; mtu:Rv1915; -.
DR   KEGG; mtv:RVBD_1915; -.
DR   PATRIC; fig|83332.111.peg.2130; -.
DR   eggNOG; COG2224; Bacteria.
DR   HOGENOM; CLU_019214_0_2_11; -.
DR   OMA; VESDWMA; -.
DR   PhylomeDB; O07718; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0004451; F:isocitrate lyase activity; IDA:MTBBASE.
DR   GO; GO:0046421; F:methylisocitrate lyase activity; IDA:MTBBASE.
DR   GO; GO:0006097; P:glyoxylate cycle; IDA:MTBBASE.
DR   GO; GO:0006102; P:isocitrate metabolic process; IDA:MTBBASE.
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; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR21631; PTHR21631; 1.
DR   Pfam; PF00463; ICL; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   1: Evidence at protein level;
KW   Lyase; Reference proteome.
FT   CHAIN           1..367
FT                   /note="Putative isocitrate lyase subunit A"
FT                   /id="PRO_0000432566"
FT   REGION          332..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        215
FT                   /evidence="ECO:0000255|PIRSR:PIRSR001362-1"
SQ   SEQUENCE   367 AA;  40490 MW;  EF3481EB46EE0796 CRC64;
     MAIAETDTEV HTPFEQDFEK DVAATQRYFD SSRFAGIIRL YTARQVVEQR GTIPVDHIVA
     REAAGAFYER LRELFAARKS ITTFGPYSPG QAVSMKRMGI EAIYLGGWAT SAKGSSTEDP
     GPDLASYPLS QVPDDAAVLV RALLTADRNQ HYLRLQMSER QRAATPAYDF RPFIIADAGT
     GHGGDPHVRN LIRRFVEVGV PGYHIEDQRP GTKKCGHQGG KVLVPSDEQI KRLNAARFQL
     DIMRVPGIIV ARTDAEAANL IDSRADERDQ PFLLGATKLD VPSYKSCFLA MVRRFTNWAS
     RSSMVIFSMR LATASTRRPA VGLSAKAFSA WSPTRSTRGG RTASSRSTAF STRSSRGSWR
     PGRTTRA
 
 
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