ID A0A100ICW5_ASPNG Unreviewed; 697 AA.
AC A0A100ICW5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Thermophilic desulfurizing enzyme family protein {ECO:0000313|EMBL:GAQ38485.1};
GN ORFNames=ABL_02684 {ECO:0000313|EMBL:GAQ38485.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ38485.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the acetate uptake transporter (AceTr) (TC
CC 2.A.96) family. {ECO:0000256|ARBA:ARBA00005587}.
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:GAQ38485.1}.
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DR EMBL; BCMY01000003; GAQ38485.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100ICW5; -.
DR PaxDb; 5061-CADANGAP00004581; -.
DR VEuPathDB; FungiDB:An04g09670; -.
DR VEuPathDB; FungiDB:An04g09680; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1159860; -.
DR VEuPathDB; FungiDB:ATCC64974_86440; -.
DR VEuPathDB; FungiDB:ATCC64974_86450; -.
DR VEuPathDB; FungiDB:M747DRAFT_268342; -.
DR VEuPathDB; FungiDB:M747DRAFT_346240; -.
DR OMA; HNWDNVG; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
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; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_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 InterPro; IPR000791; Gpr1/Fun34/SatP-like.
DR PANTHER; PTHR31123; ACCUMULATION OF DYADS PROTEIN 2-RELATED; 1.
DR PANTHER; PTHR31123:SF4; PROTEIN ALCS; 1.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF01184; Gpr1_Fun34_YaaH; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 304..397
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 530..671
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
SQ SEQUENCE 697 AA; 75608 MW; B12914C7C4D234C2 CRC64;
MSTSSPTDTK NATDAFDIER QASVSAAAAA VPVAPRTLGA GSALALGAFG TTLTTLSLSL
MEWRGVTITN VYVGNFFFIA AFGLVITAQW ELSVGNGFAY TVFSAFGLFY AGYGAILTPA
FGVAQAYGSD TAQYNNALGF FMILWTVFVF TFLIASLPIN LANIAVFFFV DLGFLTVAAS
YFADADGHAD SARALRKTGG ASCFVAGMVG WYIVFHLFLK DNSLLELPLG DTGRYFAKIT
LCHYVRSNSS QPLLNSSLSQ LTIIITTTTT MTQSDVPATD PAVYEAYKTQ WASLPDTADA
WLARAREVAT VLSQDAAQRE QENKSPRAEV ALLKHSGLLK LLGPKKYGGG EQPWSVGYKA
IREVAKGDGS IGMLLGYHLL WSTTANIVGT PSQADRIHQW IITNNYFVGG AVNPRDSDLT
ITSDGEDIIF NGAKFFNTGG VVSDLTVLEG VLDGTGEHIF ALVETRQAGI KFAHNWNNIG
LRLTESGGVK IENVRAPWTD ALGWDNVSKR PREEVLGVPF ASLLLPTIQL VFSNFYLGIA
QGALAFASQY TVSTTRPWPF GGDNKASATD EFYILERYGN FFAHLRAAEA LADRAGEEIS
TLYREHSENR PGLTARQRGE LAEWVASVKV VTTDVGLRVT SGIFEVTGAR ATAVKVGLDR
FWRDIRTHTL HDPVAYKNRE LGRYALLGEV PEPSWYT
//
