ID Q5Z108_NOCFA Unreviewed; 379 AA.
AC Q5Z108;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE SubName: Full=Putative acyl-CoA dehydrogenase {ECO:0000313|EMBL:BAD55883.1};
GN Name=fadE13 {ECO:0000313|EMBL:BAD55883.1};
GN OrderedLocusNames=NFA_10380 {ECO:0000313|EMBL:BAD55883.1};
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD55883.1, ECO:0000313|Proteomes:UP000006820};
RN [1] {ECO:0000313|EMBL:BAD55883.1, ECO:0000313|Proteomes:UP000006820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD55883.1,
RC ECO:0000313|Proteomes:UP000006820};
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD55883.1; -; Genomic_DNA.
DR RefSeq; WP_011207568.1; NC_006361.1.
DR AlphaFoldDB; Q5Z108; -.
DR STRING; 247156.NFA_10380; -.
DR GeneID; 61131860; -.
DR KEGG; nfa:NFA_10380; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_2_11; -.
DR OrthoDB; 2769798at2; -.
DR Proteomes; UP000006820; 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 InterPro; IPR001763; Rhodanese-like_dom.
DR PANTHER; PTHR43831; ISOBUTYRYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR43831:SF1; ISOBUTYRYL-COA DEHYDROGENASE, MITOCHONDRIAL; 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 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.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 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:UP000006820}.
FT DOMAIN 314..351
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 379 AA; 40685 MW; 6F56A711C3BCE268 CRC64;
MFTLDEDEKA IRDTAREFAD EFLAPNALDW DEHKHFPVDV LRKAGPLGLG GIYVHEDMGG
SGLRRLDAVR IFEQLATGCP SVAAYISIHN MATWMIDAYG SPEQRSRWLP GLTAMELLGS
YALTEPGVGS DAAALSTKAV RDGDDYILNG AKQFISGAGA NDVYVMMVRT GDDGARGISA
LIVPADTPGL SVGPNEKKMG WNAQPTRQVI LEDARVPVAN RLGAEGDGFR IAMNGLNGGR
LNIAACSVGG AQAALDKTVP YLAQRNAFGK PLLRNQALQF DLADMRTQLE AARTLLWRAA
AALDADAPDK VELCAMAKRF ATDAGFEVAN KALQLHGGYG YLAEYGLEKI VRDLRVHQIL
EGTNEIMRVV VARSVVGAA
//
