DESA2_MYCTU
ID DESA2_MYCTU Reviewed; 275 AA.
AC P9WNZ5; L0T8L4; O53442; Q7D8V3;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Putative acyl-[acyl-carrier-protein] desaturase DesA2 {ECO:0000303|PubMed:14559907, ECO:0000303|PubMed:15929999};
DE Short=Putative acyl-ACP desaturase DesA2 {ECO:0000303|PubMed:14559907};
DE EC=1.14.19.- {ECO:0000305|PubMed:14559907};
GN Name=desA2 {ECO:0000303|PubMed:14559907}; OrderedLocusNames=Rv1094;
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 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 [3]
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 [4]
RP PUPYLATION AT LYS-145, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH MANGANESE, AND
RP SUBUNIT.
RC STRAIN=H37Rv;
RX PubMed=15929999; DOI=10.1110/ps.041288005;
RA Dyer D.H., Lyle K.S., Rayment I., Fox B.G.;
RT "X-ray structure of putative acyl-ACP desaturase DesA2 from Mycobacterium
RT tuberculosis H37Rv.";
RL Protein Sci. 14:1508-1517(2005).
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:0000269|PubMed:15929999}.
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; AL123456; CCP43847.1; -; Genomic_DNA.
DR PIR; D70896; D70896.
DR RefSeq; NP_215610.1; NC_000962.3.
DR RefSeq; WP_003405801.1; NZ_NVQJ01000021.1.
DR PDB; 1ZA0; X-ray; 2.00 A; A=1-275.
DR PDBsum; 1ZA0; -.
DR AlphaFoldDB; P9WNZ5; -.
DR SMR; P9WNZ5; -.
DR STRING; 83332.Rv1094; -.
DR iPTMnet; P9WNZ5; -.
DR PaxDb; P9WNZ5; -.
DR DNASU; 885339; -.
DR GeneID; 885339; -.
DR KEGG; mtu:Rv1094; -.
DR TubercuList; Rv1094; -.
DR eggNOG; COG0208; Bacteria.
DR OMA; GYRADTY; -.
DR PhylomeDB; P9WNZ5; -.
DR BRENDA; 1.14.19.2; 3445.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000001584; Chromosome.
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; IDA:MTBBASE.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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 3D-structure; Acetylation; Fatty acid biosynthesis; Fatty acid metabolism;
KW Iron; Isopeptide bond; Lipid biosynthesis; Lipid metabolism; Metal-binding;
KW Oxidoreductase; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..275
FT /note="Putative acyl-[acyl-carrier-protein] desaturase
FT DesA2"
FT /id="PRO_0000392676"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337,
FT ECO:0000305|PubMed:15929999"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337,
FT ECO:0000305|PubMed:15929999"
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 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337,
FT ECO:0000305|PubMed:15929999"
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P22337,
FT ECO:0000305|PubMed:15929999"
FT BINDING 189
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337,
FT ECO:0000305|PubMed:15929999"
FT BINDING 192
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P22337,
FT ECO:0000305|PubMed:15929999"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CROSSLNK 145
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
FT HELIX 9..27
FT /evidence="ECO:0007829|PDB:1ZA0"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:1ZA0"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1ZA0"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1ZA0"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1ZA0"
FT HELIX 63..77
FT /evidence="ECO:0007829|PDB:1ZA0"
FT HELIX 95..120
FT /evidence="ECO:0007829|PDB:1ZA0"
FT TURN 126..130
FT /evidence="ECO:0007829|PDB:1ZA0"
FT HELIX 148..172
FT /evidence="ECO:0007829|PDB:1ZA0"
FT HELIX 176..206
FT /evidence="ECO:0007829|PDB:1ZA0"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:1ZA0"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:1ZA0"
FT HELIX 233..241
FT /evidence="ECO:0007829|PDB:1ZA0"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1ZA0"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:1ZA0"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:1ZA0"
SQ SEQUENCE 275 AA; 31359 MW; 448D136940150E99 CRC64;
MAQKPVADAL TLELEPVVEA NMTRHLDTED IWFAHDYVPF DQGENFAFLG GRDWDPSQST
LPRTITDACE ILLILKDNLA GHHRELVEHF ILEDWWGRWL GRWTAEEHLH AIALREYLVV
TREVDPVANE DVRVQHVMKG YRAEKYTQVE TLVYMAFYER CGAVFCRNLA AQIEEPILAG
LIDRIARDEV RHEEFFANLV THCLDYTRDE TIAAIAARAA DLDVLGADIE AYRDKLQNVA
DAGIFGKPQL RQLISDRITA WGLAGEPSLK QFVTG
