DESA1_MYCTU
ID DESA1_MYCTU Reviewed; 338 AA.
AC P9WNZ7; L0T7U2; Q50824; Q79FV9; Q8VKD4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Putative acyl-[acyl-carrier-protein] desaturase DesA1 {ECO:0000303|PubMed:14559907};
DE Short=Putative acyl-ACP desaturase DesA1 {ECO:0000303|PubMed:14559907};
DE EC=1.14.19.- {ECO:0000305|PubMed:14559907};
GN Name=desA1 {ECO:0000303|PubMed:14559907};
GN Synonyms=des {ECO:0000303|PubMed:9199463}; OrderedLocusNames=Rv0824c;
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 [GENOMIC DNA], ANTIGENICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
RX PubMed=9199463; DOI=10.1128/iai.65.7.2883-2889.1997;
RA Jackson M., Portnoi D., Catheline D., Dumail L., Rauzier J., Legrand P.,
RA Gicquel B.;
RT "Mycobacterium tuberculosis Des protein: an immunodominant target for the
RT humoral response of tuberculous patients.";
RL Infect. Immun. 65:2883-2889(1997).
RN [2]
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 [3]
RP SEQUENCE REVISION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12368430; DOI=10.1099/00221287-148-10-2967;
RA Camus J.-C., Pryor M.J., Medigue C., Cole S.T.;
RT "Re-annotation of the genome sequence of Mycobacterium tuberculosis
RT H37Rv.";
RL Microbiology 148:2967-2973(2002).
RN [4]
RP PUTATIVE FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=14559907; DOI=10.1074/jbc.m311209200;
RA Phetsuksiri B., Jackson M., Scherman H., McNeil M., Besra G.S.,
RA Baulard A.R., Slayden R.A., DeBarber A.E., Barry C.E. III, Baird M.S.,
RA Crick D.C., Brennan P.J.;
RT "Unique mechanism of action of the thiourea drug isoxyl on Mycobacterium
RT tuberculosis.";
RL J. Biol. Chem. 278:53123-53130(2003).
RN [5]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [6]
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: May be a desaturase involved in mycobacterial fatty acid
CC biosynthesis. {ECO:0000305|PubMed:14559907}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:P22337};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P22337};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:14559907}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WNZ5}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000305|PubMed:9199463}.
CC -!- MISCELLANEOUS: Is a major B-cell antigen. {ECO:0000269|PubMed:9199463}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000305|PubMed:19099550}.
CC -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC {ECO:0000305}.
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DR EMBL; U49839; AAB86440.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43572.1; -; Genomic_DNA.
DR PIR; H70810; H70810.
DR RefSeq; WP_003404321.1; NZ_NVQJ01000066.1.
DR RefSeq; YP_177758.1; NC_000962.3.
DR AlphaFoldDB; P9WNZ7; -.
DR SMR; P9WNZ7; -.
DR STRING; 83332.Rv0824c; -.
DR PaxDb; P9WNZ7; -.
DR PRIDE; P9WNZ7; -.
DR DNASU; 885444; -.
DR GeneID; 45424787; -.
DR GeneID; 885444; -.
DR KEGG; mtu:Rv0824c; -.
DR TubercuList; Rv0824c; -.
DR eggNOG; COG0208; Bacteria.
DR OMA; LAPNQAM; -.
DR PhylomeDB; P9WNZ7; -.
DR BRENDA; 1.14.19.2; 3445.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
DR CDD; cd01050; Acyl_ACP_Desat; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR005067; Fatty_acid_desaturase-2.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR PANTHER; PTHR31155; PTHR31155; 1.
DR Pfam; PF03405; FA_desaturase_2; 1.
DR PIRSF; PIRSF000346; Dlt9_acylACP_des; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW Fatty acid biosynthesis; Fatty acid metabolism; Iron; Lipid biosynthesis;
KW Lipid metabolism; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..338
FT /note="Putative acyl-[acyl-carrier-protein] desaturase
FT DesA1"
FT /id="PRO_0000392675"
FT REGION 314..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337"
SQ SEQUENCE 338 AA; 38770 MW; 9AC9B5A4FFBDAC20 CRC64;
MSAKLTDLQL LHELEPVVEK YLNRHLSMHK PWNPHDYIPW SDGKNYYALG GQDWDPDQSK
LSDVAQVAMV QNLVTEDNLP SYHREIAMNM GMDGAWGQWV NRWTAEENRH GIALRDYLVV
TRSVDPVELE KLRLEVVNRG FSPGQNHQGH YFAESLTDSV LYVSFQELAT RISHRNTGKA
CNDPVADQLM AKISADENLH MIFYRDVSEA AFDLVPNQAM KSLHLILSHF QMPGFQVPEF
RRKAVVIAVG GVYDPRIHLD EVVMPVLKKW RIFEREDFTG EGAKLRDELA LVIKDLELAC
DKFEVSKQRQ LDREARTGKK VSAHELHKTA GKLAMSRR
