ID A0A098S2Y5_9BACT Unreviewed; 601 AA.
AC A0A098S2Y5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KGE86391.1};
GN ORFNames=IX84_21590 {ECO:0000313|EMBL:KGE86391.1};
OS Phaeodactylibacter xiamenensis.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Haliscomenobacteraceae;
OC Phaeodactylibacter.
OX NCBI_TaxID=1524460 {ECO:0000313|EMBL:KGE86391.1, ECO:0000313|Proteomes:UP000029736};
RN [1] {ECO:0000313|EMBL:KGE86391.1, ECO:0000313|Proteomes:UP000029736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KD52 {ECO:0000313|EMBL:KGE86391.1,
RC ECO:0000313|Proteomes:UP000029736};
RX PubMed=25052393; DOI=10.1099/ijs.0.063909-0;
RA Chen Z.Jr., Lei X., Lai Q., Li Y., Zhang B., Zhang J., Zhang H., Yang L.,
RA Zheng W., Tian Y., Yu Z., Xu H.Jr., Zheng T.;
RT "Phaeodactylibacter xiamenensis gen. nov., sp. nov., a member of the family
RT Saprospiraceae isolated from the marine alga Phaeodactylum tricornutum.";
RL Int. J. Syst. Evol. Microbiol. 64:3496-3502(2014).
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}.
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:KGE86391.1}.
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DR EMBL; JPOS01000079; KGE86391.1; -; Genomic_DNA.
DR RefSeq; WP_044225179.1; NZ_JPOS01000079.1.
DR AlphaFoldDB; A0A098S2Y5; -.
DR STRING; 1524460.IX84_21590; -.
DR OrthoDB; 9764422at2; -.
DR Proteomes; UP000029736; Unassembled WGS sequence.
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; 1.
DR InterPro; IPR025878; Acyl-CoA_dh-like_C_dom.
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; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR PANTHER; PTHR42803:SF3; ACYL-COA DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF12806; Acyl-CoA_dh_C; 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:UP000029736}.
FT DOMAIN 39..155
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 161..266
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 282..449
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 468..589
FT /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12806"
SQ SEQUENCE 601 AA; 67002 MW; C3E59C38914C091A CRC64;
MAEYVNMDTL RFQLYQVHDM PQLFQYARYA EYDKDAVDIF LDSIKDFSDQ DLYPSFREMD
EAPAHFKDGK IVVHPAVGEA MKKGGELGVI GASYDMQAGG LQLPGMAFHA AYYIMEAANN
NIPGYLGLTA GAAHLIIAFG NEWLNETFVG KMLGGQWGGT MCLTEPQAGS SLSDITTTAY
PQEDGTYRIK GQKIFISGGD HEHNDNFVHL VLARIEGAPA GTKGISLFVV PKKRPEAGNL
VPNDVITAGD YQKMGQKGYC TTHLVFGENE GSTGWLVGEP HKGLKYMFQM MNEARIAVGR
GAVSIASAAY HASLQYAQER PQGRRLKNDG TKDVSEEQTL IINHPDVRRM LLLQKAIYEG
ALSVVNQTAL YHDLEMVSEG EDHEKYYLLL ELLTPIAKTY PSEKCREAVD NGLQVLGGYG
FCTDFVLQQY LRDIRIMSIY EGTTGIQSQD LLGRKVTMQK GKALEYLAAE VQKDMEAALT
YDELKPYAGM LGQKLQLVQK VLGKLMPYAM KGQYERYLSD ATLFMQMMST VVVGWQWLKM
ATAAKQALVT GDDTYTTAFY ESKVHTLKFF YKYELAKVDS LAQILMDEAV LTILEEKELI
C
//