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Database: UniProt
Entry: H6L8L8_SAPGL
LinkDB: H6L8L8_SAPGL
Original site: H6L8L8_SAPGL 
ID   H6L8L8_SAPGL            Unreviewed;       613 AA.
AC   H6L8L8;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:AFC26743.1};
GN   OrderedLocusNames=SGRA_4028 {ECO:0000313|EMBL:AFC26743.1};
OS   Saprospira grandis (strain Lewin).
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Saprospiraceae;
OC   Saprospira.
OX   NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC26743.1, ECO:0000313|Proteomes:UP000007519};
RN   [1] {ECO:0000313|EMBL:AFC26743.1, ECO:0000313|Proteomes:UP000007519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lewin {ECO:0000313|EMBL:AFC26743.1,
RC   ECO:0000313|Proteomes:UP000007519};
RX   PubMed=22675601; DOI=10.4056/sigs.2445005;
RA   Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.;
RT   "Complete genome sequencing and analysis of Saprospira grandis str. Lewin,
RT   a predatory marine bacterium.";
RL   Stand. Genomic Sci. 6:84-93(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; CP002831; AFC26743.1; -; Genomic_DNA.
DR   AlphaFoldDB; H6L8L8; -.
DR   STRING; 984262.SGRA_4028; -.
DR   KEGG; sgn:SGRA_4028; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_016513_2_1_10; -.
DR   OrthoDB; 1489360at2; -.
DR   Proteomes; UP000007519; 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; 2.40.110.20; -; 1.
DR   Gene3D; 6.10.250.600; -; 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; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR041504; AidB_N.
DR   PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42707:SF2; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF18158; AidB_N; 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.
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:UP000007519}.
FT   DOMAIN          67..220
FT                   /note="Adaptive response protein AidB N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18158"
FT   DOMAIN          230..326
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          343..495
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   613 AA;  69074 MW;  1E01F7164AA69E30 CRC64;
     MLRGSQVCSA LQAGDACLWS GPLGHPLRSA HPAGALRPVG PQKIPFPFIL VIMQKENRVL
     PRGHKTSQNY FKSDKLLEDY LHAHLPAQVL SEQSDALEQL GRLAAGVMNE LSLTADKNGP
     KLRKRNYLGE TINQIDFHPA YEELKAIAVH SGMFRLKWAP EFRERYAGQR HRLGFALGYL
     YAMSESGLYC PLCMTDGVAL LIDKYASEED KARLLPRIYT DEPKDFYTGA MFLTEKAGGS
     DVGANLVKAS PLDNGYWSLE GEKWFCSNAS AEIIFALART GPLEKGTRGL GIFLLEPQRP
     DGSANNMDLI RLKDKLGTRS MASGEYLLQG SWAKLIGEEG QDFKIMTDMI NLSRLYNSVA
     AISGLRRALI EAYQFATYRN TFGKELLEHA LVRMKFWELG SIHQGQFYSC WKAISLLDQA
     EAGDATAKEW LRFLTPMIKK ATAEQGVYVA RESMELMGGL GYIEDGVMPK VMRDIMVLPI
     WEGAGNIMIL DMLRASQKSK GLLLLLEFVY EQLKQRRGTD KLRADFALLK QKLSALAEAK
     DMDQIQLGAK QLFERLTDYF QWACISEQAS LMQTNYQELA LRYYEEERLL AQAYREQYLP
     SRAEIAGLLA WEF
//
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