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Database: UniProt
Entry: G5GBN4_9BACT
LinkDB: G5GBN4_9BACT
Original site: G5GBN4_9BACT 
ID   G5GBN4_9BACT            Unreviewed;       576 AA.
AC   G5GBN4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF9332_00985 {ECO:0000313|EMBL:EHG23233.1};
OS   Alloprevotella rava F0323.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Alloprevotella.
OX   NCBI_TaxID=679199 {ECO:0000313|EMBL:EHG23233.1, ECO:0000313|Proteomes:UP000015993};
RN   [1] {ECO:0000313|EMBL:EHG23233.1, ECO:0000313|Proteomes:UP000015993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0323 {ECO:0000313|EMBL:EHG23233.1,
RC   ECO:0000313|Proteomes:UP000015993};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA   Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella sp. oral taxon 302 str. F0323.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:EHG23233.1}.
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DR   EMBL; ACZK01000016; EHG23233.1; -; Genomic_DNA.
DR   RefSeq; WP_009347445.1; NZ_JH376829.1.
DR   AlphaFoldDB; G5GBN4; -.
DR   STRING; 679199.HMPREF9332_00985; -.
DR   PATRIC; fig|679199.3.peg.1081; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_12_2_10; -.
DR   OrthoDB; 9802867at2; -.
DR   Proteomes; UP000015993; Unassembled WGS sequence.
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; 1.20.120.470; Acyl-CoA dehydrogenase, C-terminal domain; 1.
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; IPR020964; Acyl-CoA_dehydrogenase_C.
DR   InterPro; IPR036797; Acyl-CoA_dehydrogenase_C_sf.
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   PANTHER; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 2.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   Pfam; PF12186; AcylCoA_dehyd_C; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   SUPFAM; SSF158494; PG0775 C-terminal domain-like; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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:UP000015993}.
FT   DOMAIN          92..169
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          173..268
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          283..357
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          388..444
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          452..563
FT                   /note="Acyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12186"
SQ   SEQUENCE   576 AA;  64424 MW;  961F8904A793CFB3 CRC64;
     MANCYSDHEE LKFELNHPLM KRIVELKERN FADKDKFDYA PLDYADTMDS YDRVLDIVGE
     ITATTIADNA EGVDLEGPHH EGDRVRYASG TEANLQAMVS AGMNGMTMPR RFGGLNFSIT
     PYTMCAEIVA AKDAGFGNIW SLQDCIETLY EFGNEDQHSR FIPRVCAGET MSMDLTEPDA
     GSDLQRVMLK ATYSEEKGCW LLNGVKRFIT NGDADIHLVL ARSEEGTTDG RGLSMFIYDK
     RQGGVNVRRI ENKMGIHGSP TCELVYKNAH AELCGDRKLG LIKYVMALMN GARLGIAAQS
     VGISQGAYDE ALSYAKDREQ FGKKIINFPA VYDMLALMKA KLDAGRALLY QCSRYVDIYK
     ALEDIARERK LEPEERKEQK TFAKLADSLT PLAKGMNSEY ANQNTYDGIQ ILGGSGFMMD
     YALQRYYRDA RITSIYEGTT QLQVVAAIRY VTNGSYLAQC REFETAQLSA DLQPLQTIAK
     TMADKLEEAT AKVKEAADQE LHDICARHLV EIAADTIMLH LLLYNANERP DLFAKSAHVY
     ANHVVAEVAK HHAFIMNMTP EQLAYYRQTV PAAEAE
//
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