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Database: UniProt
Entry: Q0S9N5_RHOJR
LinkDB: Q0S9N5_RHOJR
Original site: Q0S9N5_RHOJR 
ID   Q0S9N5_RHOJR            Unreviewed;       383 AA.
AC   Q0S9N5;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   24-JAN-2024, entry version 113.
DE   RecName: Full=Acyl-[acyl-carrier-protein] dehydrogenase MbtN {ECO:0000256|ARBA:ARBA00040394};
DE   AltName: Full=Mycobactin synthase protein N {ECO:0000256|ARBA:ARBA00042660};
GN   OrderedLocusNames=RHA1_ro03954 {ECO:0000313|EMBL:ABG95751.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG95751.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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:0000256|ARBA:ARBA00037085}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005102}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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DR   EMBL; CP000431; ABG95751.1; -; Genomic_DNA.
DR   RefSeq; WP_011596487.1; NC_008268.1.
DR   AlphaFoldDB; Q0S9N5; -.
DR   KEGG; rha:RHA1_ro03954; -.
DR   PATRIC; fig|101510.16.peg.3979; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_11; -.
DR   OMA; KWITGAP; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000008710; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
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; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR48083:SF20; LONG-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   PIRSF; PIRSF016578; HsaA; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125,
KW   ECO:0000313|EMBL:ABG95751.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT   DOMAIN          8..121
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          125..220
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          232..380
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   383 AA;  42267 MW;  A154BC8CBF0E55BC CRC64;
     MQRTLFDKDH EAYRETVREF LAREIEPNYE RWESERLIDR SAWLAAGKSG IVGLGVPEEF
     GGSGVTDYRF RYVVAEEIAR TATTSFGSGL SLQDDIAIPY IVNLGTEEQK QRWLPGMAAG
     ELIGAIAMTE PGAGSDLQGV KTTAVRDGVE WVINGQKTFI TNGIHSDLVI VVARTDPSAG
     SKGFSLLVVE RGMPGFSRGR KLHKVGLAGQ DTAELVFEDV RVPASNLLGT EGRGFVHLME
     NLPLERISIA VNAIAAAKAA YQWTRDYVFE RKAFGKPIGD LQNTRFALAE MLTEIEVTES
     HIDRCVLALN ADELTAVDAS KGKWWASELQ KRVVDRCVQL HGGYGYMMEY PIGRAYVDSR
     IQTIYGGTTE IMKEIIGRDI AAR
//
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