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Database: UniProt
Entry: C7M2M9_ACIFD
LinkDB: C7M2M9_ACIFD
Original site: C7M2M9_ACIFD 
ID   C7M2M9_ACIFD            Unreviewed;       404 AA.
AC   C7M2M9;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Acyl-CoA dehydrogenase domain protein {ECO:0000313|EMBL:ACU53273.1};
GN   OrderedLocusNames=Afer_0305 {ECO:0000313|EMBL:ACU53273.1};
OS   Acidimicrobium ferrooxidans (strain DSM 10331 / JCM 15462 / NBRC 103882 /
OS   ICP).
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Acidimicrobiaceae; Acidimicrobium.
OX   NCBI_TaxID=525909 {ECO:0000313|EMBL:ACU53273.1, ECO:0000313|Proteomes:UP000000771};
RN   [1] {ECO:0000313|EMBL:ACU53273.1, ECO:0000313|Proteomes:UP000000771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10331 / JCM 15462 / NBRC 103882 / ICP
RC   {ECO:0000313|Proteomes:UP000000771};
RX   PubMed=21304635; DOI=10.4056/sigs.1463;
RA   Clum A., Nolan M., Lang E., Glavina Del Rio T., Tice H., Copeland A.,
RA   Cheng J.F., Lucas S., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavrommatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Goker M., Spring S., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Chain P., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Acidimicrobium ferrooxidans type strain
RT   (ICP).";
RL   Stand. Genomic Sci. 1:38-45(2009).
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}.
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DR   EMBL; CP001631; ACU53273.1; -; Genomic_DNA.
DR   RefSeq; WP_015797774.1; NC_013124.1.
DR   AlphaFoldDB; C7M2M9; -.
DR   STRING; 525909.Afer_0305; -.
DR   GeneID; 80814466; -.
DR   KEGG; afo:Afer_0305; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_11; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000000771; Chromosome.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000771}.
FT   DOMAIN          9..115
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          126..223
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          254..398
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   404 AA;  44253 MW;  073BF3C242EC102A CRC64;
     MEPFSLALTD EQQQLREWAH TFAAETIRPA AHEWDEREET PRPIIEEAAR IGLYSYDFML
     NAFADKTGLT MPLVLEELCW GDAGITLAIF GSTLAVSGIV ANGTPEQIAE WVPQCFGTAD
     HPNLAAFCVS EPDAGSDVSS LRTRAVYDPA TDTWTLNGTK TWITNGGIAD IHVVVASVEP
     ELGARGQASF VIAPNTPGLR MGQKFKKMGI RASHTAEVIL EDVRLPGSAL LGGKERLDER
     LARAREGKRA QSQAAMATFE ASRPLVGAQA VGIARAAYEW ALDYAKERVQ FGRPIIENQG
     IAFKLADMAL AVDTARLLVH RAAWMAAQGQ RFEHAEGSMA KLHAGEVAVR VTEEAIQILG
     GYGYVRENPV ERWHRDAKIY TIFEGTSEIQ RLIIARAISG MRLR
//
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