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Y1425_MYCTU
ID   Y1425_MYCTU             Reviewed;         459 AA.
AC   P9WKC1; L0T9D0; O06833; P71694;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Putative diacyglycerol O-acyltransferase Rv1425;
DE            EC=2.3.1.20 {ECO:0000250|UniProtKB:P9WKC9};
DE   AltName: Full=Putative triacylglycerol synthase Rv1425;
GN   OrderedLocusNames=Rv1425; ORFNames=MTCY21B4.43, MTCY493.29c;
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   EXPRESSION IN E.COLI, AND INDUCTION.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=15262939; DOI=10.1128/jb.186.15.5017-5030.2004;
RA   Daniel J., Deb C., Dubey V.S., Sirakova T.D., Abomoelak B., Morbidoni H.R.,
RA   Kolattukudy P.E.;
RT   "Induction of a novel class of diacylglycerol acyltransferases and
RT   triacylglycerol accumulation in Mycobacterium tuberculosis as it goes into
RT   a dormancy-like state in culture.";
RL   J. Bacteriol. 186:5017-5030(2004).
RN   [3]
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: Upon expression in E.coli functions very weakly as a
CC       triacylglycerol synthase, making triacylglycerol (TG) from diolein and
CC       long-chain fatty acyl-CoA. Has no wax synthase activity.
CC       {ECO:0000269|PubMed:15262939}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC         + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC         Evidence={ECO:0000250|UniProtKB:P9WKC9};
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC   -!- INDUCTION: Constitutively expressed at a low level, it is not further
CC       induced by hypoxia or nitric oxide exposure.
CC       {ECO:0000269|PubMed:15262939}.
CC   -!- SIMILARITY: Belongs to the long-chain O-acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP44184.1; -; Genomic_DNA.
DR   PIR; D70914; D70914.
DR   RefSeq; NP_215941.1; NC_000962.3.
DR   RefSeq; WP_003898875.1; NZ_NVQJ01000038.1.
DR   AlphaFoldDB; P9WKC1; -.
DR   SMR; P9WKC1; -.
DR   STRING; 83332.Rv1425; -.
DR   PaxDb; P9WKC1; -.
DR   DNASU; 886668; -.
DR   GeneID; 886668; -.
DR   KEGG; mtu:Rv1425; -.
DR   TubercuList; Rv1425; -.
DR   eggNOG; COG1020; Bacteria.
DR   OMA; RNLAPIN; -.
DR   PhylomeDB; P9WKC1; -.
DR   UniPathway; UPA00282; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0047196; F:long-chain-alcohol O-fatty-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0001666; P:response to hypoxia; IBA:GO_Central.
DR   GO; GO:0071731; P:response to nitric oxide; IBA:GO_Central.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR014292; Acyl_transf_WS/DGAT.
DR   InterPro; IPR045034; O-acyltransferase_WSD1-like.
DR   InterPro; IPR009721; O-acyltransferase_WSD1_C.
DR   InterPro; IPR004255; O-acyltransferase_WSD1_N.
DR   PANTHER; PTHR31650; PTHR31650; 1.
DR   Pfam; PF03007; WES_acyltransf; 1.
DR   Pfam; PF06974; WS_DGAT_C; 1.
DR   TIGRFAMs; TIGR02946; acyl_WS_DGAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Glycerol metabolism; Lipid biosynthesis; Lipid metabolism;
KW   Reference proteome; Transferase.
FT   CHAIN           1..459
FT                   /note="Putative diacyglycerol O-acyltransferase Rv1425"
FT                   /id="PRO_0000222908"
FT   ACT_SITE        138
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   459 AA;  50063 MW;  F436D6B588562263 CRC64;
     MKRLSSVDAA FWSAETAGWH MHVGALAICD PSDAPEYSFQ RLRELIIERL PEIPQLRWRV
     TGAPLGLDRP WFVEDEELDI DFHIRRIGVP APGGRRELEE LVGRLMSYKL DRSRPLWELW
     VIEGVEGGRI ATLTKMHHAI VDGVSGAGLG EILLDITPEP RPPQQETVGF VGFQIPGLER
     RAIGALINVG IMTPFRIVRL LEQTVRQQIA ALGVAGKPAR YFEAPKTRFN APVSPHRRVT
     GTRVELARAK AVKDAFGVKL NDVVLALVAG AARQYLQKRD ELPAKPLIAQ IPVSTRSEET
     KADVGNQVSS MTASLATHIE DPAKRLAAIH ESTLSAKEMA KAPSAHQIMG LTETTPPGLL
     QLAARAYTAS GLSHNLAPIN LVVSNVPGPP FPLYMAGARL DSLVPLGPPV MDVALNITCF
     SYQDYLDFGL VTTPEVANDI DEMADAIEPA LAELERAAE
 
 
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