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Database: UniProt
Entry: A0A101ALZ6_9MYCO
LinkDB: A0A101ALZ6_9MYCO
Original site: A0A101ALZ6_9MYCO 
ID   A0A101ALZ6_9MYCO        Unreviewed;       412 AA.
AC   A0A101ALZ6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KUI25346.1};
GN   ORFNames=AU194_00130 {ECO:0000313|EMBL:KUI25346.1};
OS   Mycobacterium sp. GA-2829.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1772283 {ECO:0000313|EMBL:KUI25346.1, ECO:0000313|Proteomes:UP000053444};
RN   [1] {ECO:0000313|EMBL:KUI25346.1, ECO:0000313|Proteomes:UP000053444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GA-2829 {ECO:0000313|EMBL:KUI25346.1,
RC   ECO:0000313|Proteomes:UP000053444};
RG   TB Trials Study Group;
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E.L., Macaden R.,
RA   Grewal H.M.S.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
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:KUI25346.1}.
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DR   EMBL; LQIT01000056; KUI25346.1; -; Genomic_DNA.
DR   RefSeq; WP_059092110.1; NZ_LQIT01000056.1.
DR   AlphaFoldDB; A0A101ALZ6; -.
DR   STRING; 1772283.AU194_00130; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000053444; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   CDD; cd00567; ACAD; 1.
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; 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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF42; SHORT-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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.
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:UP000053444}.
FT   DOMAIN          47..145
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          149..244
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          256..406
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   412 AA;  46944 MW;  7B41474904152582 CRC64;
     MDFTLPEHLP GLLEEMDAFI EAEIKPLERE HIQYFDRHRE YARTDWENGG IPQRAWEDLL
     DEMRRCADAA GWLRYGLPAQ FGGRDGSNID MAVIREHLAH KGLGLHNDLQ DESSIVGNFP
     QVIMMDRFGT DAQKAEWIEA MITGKRSMAF GLTEPDHGSD ATWLETRAVR DGDGWVINGT
     KRWNTGVHRA THDLIFARTS GEPGQARGIT AFLVPTDTPG FEVPYYWWTF NMPTDHGEVV
     LTDVRVPDDA ILGEVDRGLE VGQTFLHENR IRQAASSLGA AQYCIDRAVD YAGQRTVFGK
     PLAVNQAVQW PLVELQTEAQ MVRLLVYYAA TELDRSHHME VSDKVSMANY RANRLVCEAA
     DRAMQVHGGV GYSRHEPFEH IYRHHRRYRI TEGAEEIQIR RVAQRLFGFG RK
//
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