ID I0XV65_9LEPT Unreviewed; 575 AA.
AC I0XV65;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Acyl-CoA dehydrogenase, C-terminal domain protein {ECO:0000313|EMBL:EIE02773.1};
GN ORFNames=LEP1GSC185_0827 {ECO:0000313|EMBL:EIE02773.1};
OS Leptospira licerasiae serovar Varillal str. VAR 010.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049972 {ECO:0000313|EMBL:EIE02773.1, ECO:0000313|Proteomes:UP000004889};
RN [1] {ECO:0000313|EMBL:EIE02773.1, ECO:0000313|Proteomes:UP000004889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VAR 010 {ECO:0000313|EMBL:EIE02773.1};
RX PubMed=23145189; DOI=10.1371/journal.pntd.0001853;
RA Ricaldi J.N., Fouts D.E., Selengut J.D., Harkins D.M., Patra K.P.,
RA Moreno A., Lehmann J.S., Purushe J., Sanka R., Torres M., Webster N.J.,
RA Vinetz J.M., Matthias M.A.;
RT "Whole Genome Analysis of Leptospira licerasiae Provides Insight into
RT Leptospiral Evolution and Pathogenicity.";
RL PLoS Negl. Trop. Dis. 6:E1853-E1853(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {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:EIE02773.1}.
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DR EMBL; AHOO02000005; EIE02773.1; -; Genomic_DNA.
DR RefSeq; WP_008590451.1; NZ_AHOO02000005.1.
DR AlphaFoldDB; I0XV65; -.
DR PATRIC; fig|1049972.3.peg.141; -.
DR OrthoDB; 9771038at2; -.
DR Proteomes; UP000004889; 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; 2.40.110.20; -; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
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.
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}.
FT DOMAIN 26..180
FT /note="Adaptive response protein AidB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18158"
FT DOMAIN 195..287
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 305..437
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
SQ SEQUENCE 575 AA; 65304 MW; 99A64E6E2B5F45E8 CRC64;
MNHPLRLAEN PGLSSYDLTG YKGNRGKNFY EEDKILQRIV ERYSSDYKPD HKKAMIDHLK
GYGELVGGIL DELTEASHKE GKYGEVVKYD RTGNRIDQIV YSHEQKLSRK ISYDYGIVNL
DFHDEWKFPF TDLHRQALTY LANQNGEGGV TCPLAMTEGM IRVLQGIGTE EQKKKYLPLV
AGKGSFSHFM AGQYVTERVG GSNVGANRTI ARKGEDGKWI LNGEKWFCSN PGDLWVTTAK
IEDTETVGLF LVPRIKDNGE LNGHHILRKK DIIGSKGKLT VEIVYEDLEA EALGRPAHGI
ANLIRYVIRT SRVHVGLAAS GMSRRAFMEA REYSRYRTAY GKKIQDFPAY SRELAEIRIL
YAALVMPIFR GIDWAQKGIL AEQISTPLMK YRSSSLSSQI THRAIMALGG SGIIGDYTCL
PRLHNDCIIN ETWEGTHLII TDHALGAMNR VKIRDSFVLE LKKNFDSAKK YPELKAVAEL
GENFLLDWNK NIEEKPREWK ETYRVDLSDQ AYGALVLSEF LEQAVFDRAS GSKRSRFDSF
AKGFGAFLFR TLPKTFGDYE SFRLDQEEVD EIVNW
//