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Database: UniProt
Entry: A0A0D1K1G8_9MYCO
LinkDB: A0A0D1K1G8_9MYCO
Original site: A0A0D1K1G8_9MYCO 
ID   A0A0D1K1G8_9MYCO        Unreviewed;       383 AA.
AC   A0A0D1K1G8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
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   ORFNames=TL10_00605 {ECO:0000313|EMBL:KIU18784.1};
OS   Mycolicibacterium llatzerense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=280871 {ECO:0000313|EMBL:KIU18784.1, ECO:0000313|Proteomes:UP000032221};
RN   [1] {ECO:0000313|EMBL:KIU18784.1, ECO:0000313|Proteomes:UP000032221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLUC14 {ECO:0000313|EMBL:KIU18784.1,
RC   ECO:0000313|Proteomes:UP000032221};
RA   Greninger A.L., Langelier C., Cunningham G., Chiu C.Y., Miller S.;
RT   "Genome sequence of Mycobacterium llatzerense and Mycobacterium immunogenum
RT   recovered from brain abscess.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIU18784.1}.
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DR   EMBL; JXST01000001; KIU18784.1; -; Genomic_DNA.
DR   RefSeq; WP_043390715.1; NZ_LXSC01000004.1.
DR   AlphaFoldDB; A0A0D1K1G8; -.
DR   STRING; 280871.TL10_00605; -.
DR   PATRIC; fig|280871.6.peg.121; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000032221; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000032221}.
FT   DOMAIN          7..121
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          125..219
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;  42848 MW;  906352F69438E19C CRC64;
     MERTLYTADH TAYRETVREF LAREVVPHQH DWDRDRWIDR AVFARAAKAG IYALQIDEQY
     GGAGESDYRY RMVVCEEVSR INALSFGLTV SLQDDLVLHY LLDLTNDEQK QRWLPGFAAG
     EIIGALAMTE PGAGSDLRGI RTTARREGDT WILNGQKTFI SSGIMSDLVV VAARTDPEAG
     SRGFSLFVVE RDTPGFERGR KLDKIGLPAQ DTAELYFRDA EVPATNLLGE AGMGLPYLMS
     HLPRERLGVS AKAIATTRAI FSSTVDYCRQ RQAFGKPLTD KQHIRFELAE MSTEIDIAES
     YVDRSVLAYN AGTLSAIDAA KGKWYVSELQ KRVIDRCLQL HGGYGYMTEY PVARAYLDTR
     IQTIYGGTTE IMKEIIGRDI AAC
//
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