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Database: UniProt
Entry: A0A098S2Y5_9BACT
LinkDB: A0A098S2Y5_9BACT
Original site: A0A098S2Y5_9BACT 
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
//
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