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Database: UniProt
Entry: D6ZB27_SEGRD
LinkDB: D6ZB27_SEGRD
Original site: D6ZB27_SEGRD 
ID   D6ZB27_SEGRD            Unreviewed;       395 AA.
AC   D6ZB27;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Acyl-CoA dehydrogenase type 2 domain protein {ECO:0000313|EMBL:ADG96786.1};
GN   OrderedLocusNames=Srot_0299 {ECO:0000313|EMBL:ADG96786.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM
OS   44985 / JCM 13578).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96786.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96786.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M., Schneider S.,
RA   Bruce D., Goodwin L., Pitluck S., Liolios K., Mikhailova N., Pati A.,
RA   Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chertkov O., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Detter J.C., Han C.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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DR   EMBL; CP001958; ADG96786.1; -; Genomic_DNA.
DR   RefSeq; WP_013137242.1; NC_014168.1.
DR   AlphaFoldDB; D6ZB27; -.
DR   STRING; 640132.Srot_0299; -.
DR   KEGG; srt:Srot_0299; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_2_0_11; -.
DR   OMA; IKDTWHV; -.
DR   OrthoDB; 3404950at2; -.
DR   Proteomes; UP000002247; Chromosome.
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; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR48083:SF19; FLAVIN-DEPENDENT MONOOXYGENASE, OXYGENASE SUBUNIT HSAA; 1.
DR   PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF08028; Acyl-CoA_dh_2; 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   Reference proteome {ECO:0000313|Proteomes:UP000002247}.
FT   DOMAIN          243..371
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08028"
SQ   SEQUENCE   395 AA;  42309 MW;  231898A780F34FD6 CRC64;
     MTTFDTITAA DVLDRVRDLL PLIREHAAQN ERDRKIADEV IAALRDAGAF RLAAPRRFGG
     LEAGLRAMLD LSALIAEADG GTSWVTTLSN INAWSTCLYD AATVDEIYAD GPDAILSGVV
     SPGGTARATP GGYLIRGEWP YCSASLHADW VSGGVWEVDE NGDEIDQSMV VMRASDVQIK
     DTWHVAGMRS SGSNTIVADD VFVPSHRVSS MLPVVSGDSV EQYPDNPFYR SAFAPMLVLV
     LIGPQLGLGR AALDIAVKKA STKALAYTNI EQQADSVAFQ LLVADAATKI DTAHLHAYRA
     ADDVERYAEQ GVYPDVAARA RMRADAAVAL TSVNDAINTL LNACGAGSFA DVNPLQRIWR
     DANVGQRHAV ILPQVSMETY GKALLGRTDH ITAIL
//
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