MBTN_MYCTU
ID MBTN_MYCTU Reviewed; 386 AA.
AC P9WQF9; L0T946; P63431; Q11016;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Acyl-[acyl-carrier-protein] dehydrogenase MbtN;
DE Short=Acyl-ACP dehydrogenase MbtN;
DE EC=1.3.99.-;
DE AltName: Full=Mycobactin synthase protein N;
GN Name=mbtN; Synonyms=fadE14; OrderedLocusNames=Rv1346;
GN ORFNames=MTCY02B10.10;
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 INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12065475; DOI=10.1128/iai.70.7.3371-3381.2002;
RA Rodriguez G.M., Voskuil M.I., Gold B., Schoolnik G.K., Smith I.;
RT "IdeR, an essential gene in Mycobacterium tuberculosis: role of IdeR in
RT iron-dependent gene expression, iron metabolism, and oxidative stress
RT response.";
RL Infect. Immun. 70:3371-3381(2002).
RN [3]
RP FUNCTION, ROLE IN MYCOBACTIN BIOSYNTHESIS, AND COFACTOR.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16461464; DOI=10.1073/pnas.0507924103;
RA Krithika R., Marathe U., Saxena P., Ansari M.Z., Mohanty D., Gokhale R.S.;
RT "A genetic locus required for iron acquisition in Mycobacterium
RT tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2069-2074(2006).
RN [4]
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: Catalyzes the dehydrogenation at the alpha-beta position of
CC ACP-bound acyl chains. This results in the introduction of a double
CC bond in the lipidic chain, which is further transferred to the epsilon-
CC amino group of lysine residue in the mycobactin core by MbtK.
CC {ECO:0000269|PubMed:16461464}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:16461464};
CC -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC -!- INDUCTION: Induced by iron starvation conditions. Transcriptionally
CC repressed by IdeR and iron. {ECO:0000269|PubMed:12065475}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44104.1; -; Genomic_DNA.
DR PIR; A70740; A70740.
DR RefSeq; NP_215862.1; NC_000962.3.
DR RefSeq; WP_003406953.1; NZ_NVQJ01000031.1.
DR PDB; 4XVX; X-ray; 2.30 A; A/B=2-386.
DR PDBsum; 4XVX; -.
DR AlphaFoldDB; P9WQF9; -.
DR SMR; P9WQF9; -.
DR STRING; 83332.Rv1346; -.
DR SwissLipids; SLP:000001256; -.
DR PaxDb; P9WQF9; -.
DR DNASU; 886844; -.
DR GeneID; 45425324; -.
DR GeneID; 886844; -.
DR KEGG; mtu:Rv1346; -.
DR TubercuList; Rv1346; -.
DR eggNOG; COG1960; Bacteria.
DR OMA; MMTRRQF; -.
DR PhylomeDB; P9WQF9; -.
DR BioCyc; MetaCyc:G185E-5525-MON; -.
DR UniPathway; UPA00011; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IDA:MTBBASE.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0019540; P:catechol-containing siderophore biosynthetic process; IDA:MTBBASE.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..386
FT /note="Acyl-[acyl-carrier-protein] dehydrogenase MbtN"
FT /id="PRO_0000000538"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 77..96
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:4XVX"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:4XVX"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:4XVX"
FT STRAND 142..153
FT /evidence="ECO:0007829|PDB:4XVX"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:4XVX"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:4XVX"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:4XVX"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:4XVX"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4XVX"
FT STRAND 205..215
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:4XVX"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:4XVX"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 226..262
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 274..299
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 305..329
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:4XVX"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 342..349
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:4XVX"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 359..368
FT /evidence="ECO:0007829|PDB:4XVX"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:4XVX"
SQ SEQUENCE 386 AA; 41180 MW; 60A2765380F89EFB CRC64;
MTAGSDLDDF RGLLAKAFDE RVVAWTAEAE AQERFPRQLI EHLGVCGVFD AKWATDARPD
VGKLVELAFA LGQLASAGIG VGVSLHDSAI AILRRFGKSD YLRDICDQAI RGAAVLCIGA
SEESGGSDLQ IVETEIRSRD GGFEVRGVKK FVSLSPIADH IMVVARSVDH DPTSRHGNVA
VVAVPAAQVS VQTPYRKVGA GPLDTAAVCI DTWVPADALV ARAGTGLAAI SWGLAHERMS
IAGQIAASCQ RAIGITLARM MSRRQFGQTL FEHQALRLRM ADLQARVDLL RYALHGIAEQ
GRLELRTAAA VKVTAARLGE EVISECMHIF GGAGYLVDET TLGKWWRDMK LARVGGGTDE
VLWELVAAGM TPDHDGYAAV VGASKA
