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ACEAB_MYCTU
ID   ACEAB_MYCTU             Reviewed;         398 AA.
AC   O07717; F2GH79; I6XZA6; L0T891;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Putative isocitrate lyase subunit B {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=aceAb; OrderedLocusNames=Rv1916, RVBD_1916;
GN   ORFNames=LH57_10435, P425_01981;
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.
CC   -!- FUNCTION: Together with AceAa, 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; CCP44683.1; -; Genomic_DNA.
DR   EMBL; CP003248; AFN49848.1; -; Genomic_DNA.
DR   EMBL; JLDD01000021; KBJ34150.1; -; Genomic_DNA.
DR   EMBL; CP009480; AIR14661.1; -; Genomic_DNA.
DR   RefSeq; NP_216432.1; NC_000962.3.
DR   RefSeq; WP_003903680.1; NZ_NVQJ01000034.1.
DR   AlphaFoldDB; O07717; -.
DR   SMR; O07717; -.
DR   STRING; 83332.Rv1916; -.
DR   PaxDb; O07717; -.
DR   DNASU; 885383; -.
DR   GeneID; 885383; -.
DR   KEGG; mtu:Rv1916; -.
DR   KEGG; mtv:RVBD_1916; -.
DR   PATRIC; fig|83332.111.peg.2131; -.
DR   eggNOG; COG2224; Bacteria.
DR   HOGENOM; CLU_692273_0_0_11; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0004451; F:isocitrate lyase activity; IBA:GO_Central.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.60; -; 1.
DR   InterPro; IPR006254; Isocitrate_lyase.
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.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..398
FT                   /note="Putative isocitrate lyase subunit B"
FT                   /id="PRO_0000432567"
SQ   SEQUENCE   398 AA;  44582 MW;  13337630E272E67F CRC64;
     MTYGEAVADV LEFGQSEGEP IGMAPEEWRA FAARASLHAA RAKAKELGAD PPWDCELAKT
     PEGYYQIRGG IPYAIAKSLA AAPFADILWM ETKTADLADA RQFAEAIHAE FPDQMLAYNL
     SPSFNWDTTG MTDEEMRRFP EELGKMGFVF NFITYGGHQI DGVAAEEFAT ALRQDGMLAL
     ARLQRKMRLV ESPYRTPQTL VGGPRSDAAL AASSGRTATT KAMGKGSTQH QHLVQTEVPR
     KLLEEWLAMW SGHYQLKDKL RVQLRPQRAG SEVLELGIHG ESDDKLANVI FQPIQDRRGR
     TILLVRDQNT FGAELRQKRL MTLIHLWLVH RFKAQAVHYV TPTDDNLYQT SKMKSHGIFT
     EVNQEVGEII VAEVNHPRIA ELLTPDRVAL RKLITKEA
 
 
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