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Database: UniProt
Entry: H6RAM7_NOCCG
LinkDB: H6RAM7_NOCCG
Original site: H6RAM7_NOCCG 
ID   H6RAM7_NOCCG            Unreviewed;       650 AA.
AC   H6RAM7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:CCF66238.1};
GN   OrderedLocusNames=NOCYR_5491 {ECO:0000313|EMBL:CCF66238.1};
OS   Nocardia cyriacigeorgica (strain GUH-2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF66238.1, ECO:0000313|Proteomes:UP000008190};
RN   [1] {ECO:0000313|EMBL:CCF66238.1, ECO:0000313|Proteomes:UP000008190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GUH-2 {ECO:0000313|EMBL:CCF66238.1,
RC   ECO:0000313|Proteomes:UP000008190};
RX   PubMed=22461543; DOI=10.1128/JB.00161-12;
RA   Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L.,
RA   Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S.,
RA   Nazaret S., Neto M., Petit S., Roche D., Vallenet D., Rodriguez-Nava V.,
RA   Richard Y., Cournoyer B., Blaha D.;
RT   "Genome sequence of the human- and animal-pathogenic strain Nocardia
RT   cyriacigeorgica GUH-2.";
RL   J. Bacteriol. 194:2098-2099(2012).
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; FO082843; CCF66238.1; -; Genomic_DNA.
DR   RefSeq; WP_014353682.1; NC_016887.1.
DR   AlphaFoldDB; H6RAM7; -.
DR   STRING; 1127134.NOCYR_5491; -.
DR   KEGG; ncy:NOCYR_5491; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_11_1_11; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000008190; Chromosome.
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   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; 2.
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.
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:UP000008190}.
FT   DOMAIN          66..165
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          169..267
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          279..438
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   650 AA;  70662 MW;  C2F11A7482CEAB8A CRC64;
     MATTAKVDAT EEQARALVEE SRETGWAKPS FAKEMFLGRF RLDLIHPYPR PTAEDADRTD
     EFLARLRPVC ASMDGTVIEE QSRIPDDYVR SLADLGCFGL KIPPDYGGQG LSQYGYNRAL
     MLVGSAHPSL GVLLSAHQSI GVPEPLKLAG TEEQKREFLP RCAAGAVSAF LLTEPDVGSD
     PARMASTATP TEDGEAYELN GVKLWTTNGV VAELLVVMAR VPKSEGHRGG ISAFVVEADS
     PGLTVERRNS FMGLHGIENG VTRMHNVRVP ARNLIGREGD GLKIALTTLN AGRLAIPALC
     TAASKWSLKI AREWSTQRVQ WGRPVGEHAA VGAKLSFIAA TTFALEAVLD LSATMADEGR
     NDIRIEAALA KLWSSEMSCR IADELVQIRG GRGYETAASL AARGERAVPA EQLVRDLRIN
     RIFEGSSEIM RLLIAREMAD AHMAAAGALV DRNAGLEDKA KAAIGAGGFY AKWFPQLAVG
     AGTVPASYPE FGPLAKHLRF VERNARKQAR SLMYAMARWQ AGLEYRQNFL GRIVDIGAEL
     FAMSAACVRA QDLRTSGAVE ARSATELADT FCQQARLRVK ALFDALWDNT DDEDRALTRG
     ILDGNHEWLE DGVLDQSEGT GPWIAEWQFG PSTETNLLRP FLPSTRRVGT
//
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