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LIPB_MYCTU
ID   LIPB_MYCTU              Reviewed;         230 AA.
AC   P9WK83; L0T8Z0; Q10404;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
DE            EC=2.3.1.181 {ECO:0000255|HAMAP-Rule:MF_00013};
DE   AltName: Full=Lipoate-protein ligase B {ECO:0000255|HAMAP-Rule:MF_00013};
DE   AltName: Full=Lipoyl/octanoyl transferase {ECO:0000255|HAMAP-Rule:MF_00013};
DE   AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase {ECO:0000255|HAMAP-Rule:MF_00013};
GN   Name=lipB {ECO:0000255|HAMAP-Rule:MF_00013}; OrderedLocusNames=Rv2217;
GN   ORFNames=MTCY190.28;
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   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).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP   FUNCTION, REACTION MECHANISM, SUBUNIT, AND MUTAGENESIS OF LYS-142 AND
RP   CYS-176.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=16735476; DOI=10.1073/pnas.0510436103;
RA   Ma Q., Zhao X., Eddine A.N., Geerlof A., Li X., Cronan J.E.,
RA   Kaufmann S.H.E., Wilmanns M.;
RT   "The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine
RT   dyad acyltransferase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:8662-8667(2006).
CC   -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid
CC       from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-
CC       dependent enzymes. Lipoyl-ACP can also act as a substrate although
CC       octanoyl-ACP is likely to be the physiological substrate.
CC       {ECO:0000255|HAMAP-Rule:MF_00013, ECO:0000269|PubMed:16735476}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-
CC         octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-
CC         COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00013};
CC   -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC       pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC       protein]: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00013}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16735476}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00013}.
CC   -!- MISCELLANEOUS: In the reaction, the free carboxyl group of octanoic
CC       acid is attached via an amide linkage to the epsilon-amino group of a
CC       specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
CC   -!- SIMILARITY: Belongs to the LipB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00013}.
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DR   EMBL; AL123456; CCP44994.1; -; Genomic_DNA.
DR   PIR; B70787; B70787.
DR   RefSeq; NP_216733.1; NC_000962.3.
DR   RefSeq; WP_003411458.1; NZ_NVQJ01000008.1.
DR   PDB; 1W66; X-ray; 1.08 A; A=3-230.
DR   PDBsum; 1W66; -.
DR   AlphaFoldDB; P9WK83; -.
DR   SMR; P9WK83; -.
DR   STRING; 83332.Rv2217; -.
DR   DrugBank; DB03600; Capric acid.
DR   PaxDb; P9WK83; -.
DR   DNASU; 887626; -.
DR   GeneID; 45426193; -.
DR   GeneID; 887626; -.
DR   KEGG; mtu:Rv2217; -.
DR   TubercuList; Rv2217; -.
DR   eggNOG; COG0321; Bacteria.
DR   OMA; GEVTYHC; -.
DR   PhylomeDB; P9WK83; -.
DR   BRENDA; 2.3.1.181; 3445.
DR   BRENDA; 6.3.1.20; 3445.
DR   UniPathway; UPA00538; UER00592.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IDA:MTBBASE.
DR   GO; GO:0009107; P:lipoate biosynthetic process; IMP:MTBBASE.
DR   GO; GO:0009249; P:protein lipoylation; IBA:GO_Central.
DR   CDD; cd16444; LipB; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00013; LipB; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004143; BPL_LPL_catalytic.
DR   InterPro; IPR000544; Octanoyltransferase.
DR   InterPro; IPR020605; Octanoyltransferase_CS.
DR   PIRSF; PIRSF016262; LPLase; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00214; lipB; 1.
DR   PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
DR   PROSITE; PS01313; LIPB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..230
FT                   /note="Octanoyltransferase"
FT                   /id="PRO_0000062851"
FT   DOMAIN          38..215
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT   ACT_SITE        176
FT                   /note="Acyl-thioester intermediate"
FT   BINDING         76..83
FT                   /ligand="substrate"
FT   BINDING         145..147
FT                   /ligand="substrate"
FT   BINDING         158..160
FT                   /ligand="substrate"
FT   SITE            142
FT                   /note="Lowers pKa of active site Cys"
FT   MUTAGEN         142
FT                   /note="K->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:16735476"
FT   MUTAGEN         176
FT                   /note="C->S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:16735476"
FT   STRAND          13..19
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   HELIX           22..37
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   STRAND          43..48
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   STRAND          51..55
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   HELIX           61..63
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   STRAND          75..83
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   STRAND          87..93
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   HELIX           102..119
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   STRAND          130..135
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   STRAND          141..151
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   STRAND          154..164
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   HELIX           168..172
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   HELIX           175..177
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   STRAND          179..183
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   HELIX           186..190
FT                   /evidence="ECO:0007829|PDB:1W66"
FT   HELIX           196..211
FT                   /evidence="ECO:0007829|PDB:1W66"
SQ   SEQUENCE   230 AA;  24211 MW;  E967D3EBD338FE61 CRC64;
     MTGSIRSKLS AIDVRQLGTV DYRTAWQLQR ELADARVAGG ADTLLLLEHP AVYTAGRRTE
     THERPIDGTP VVDTDRGGKI TWHGPGQLVG YPIIGLAEPL DVVNYVRRLE ESLIQVCADL
     GLHAGRVDGR SGVWLPGRPA RKVAAIGVRV SRATTLHGFA LNCDCDLAAF TAIVPCGISD
     AAVTSLSAEL GRTVTVDEVR ATVAAAVCAA LDGVLPVGDR VPSHAVPSPL
 
 
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