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Database: UniProt
Entry: A0A0F4Z2M2_TALEM
LinkDB: A0A0F4Z2M2_TALEM
Original site: A0A0F4Z2M2_TALEM 
ID   A0A0F4Z2M2_TALEM        Unreviewed;       445 AA.
AC   A0A0F4Z2M2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Thermophilic desulfurizing enzyme family protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=T310_1616 {ECO:0000313|EMBL:KKA24331.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA24331.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA24331.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA24331.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKA24331.1}.
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DR   EMBL; LASV01000065; KKA24331.1; -; Genomic_DNA.
DR   RefSeq; XP_013330943.1; XM_013475489.1.
DR   AlphaFoldDB; A0A0F4Z2M2; -.
DR   STRING; 1408163.A0A0F4Z2M2; -.
DR   GeneID; 25313967; -.
DR   OrthoDB; 2264654at2759; -.
DR   Proteomes; UP000053958; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   PANTHER; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF08028; Acyl-CoA_dh_2; 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.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        272..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          64..146
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          279..419
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   445 AA;  48901 MW;  3CD133003E7173C9 CRC64;
     MAQVPVPEKI AVLQSKAVPN PAPPATDPKV YQEHHDAFAA EGLPKTPEAW LERAKKVSDI
     LAVDAAARNK EQKTPRAEVA LLKSSGLTKI LGDPKYGGGG QNWDTALKCV RQVAIGDGSI
     GMLLGYHLMW SRIAAIVGTE EQRERYEKLI NENNYYVGGA VNPRDNDSVI AEAGGKLVLN
     GFKNFTTGAA VSDLVVLEGV YDGAEDHIFA LVPTNQPGIV FLNNWNNMGL RLTESGAAKL
     MQVNFPWEDA LGWNTETKTA IKELVAGPFS TIMVPIIQLV FANFYIGIAY GALRTGSEYT
     KTQTRAWPFS HDPKSSPLEE HYILARYGKS FASLKAAEAL ADKAGDELAA LFAAHGVSRD
     ITERQRGDLA ELVTALKIVV THTCLEVTSS IFEVTGSRST SERYGFDRFW KDIRTHTLHD
     PVAYKETELG RYYLLDEIPK PSWYT
//
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