ACDB_BACSU
ID ACDB_BACSU Reviewed; 379 AA.
AC P45857;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Acyl-CoA dehydrogenase;
DE EC=1.3.99.-;
GN Name=mmgC; Synonyms=yqiN; OrderedLocusNames=BSU24150;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=168 / MB24;
RX PubMed=8759838; DOI=10.1128/jb.178.16.4778-4786.1996;
RA Bryan E.M., Beall B.W., Moran C.P. Jr.;
RT "A sigma E dependent operon subject to catabolite repression during
RT sporulation in Bacillus subtilis.";
RL J. Bacteriol. 178:4778-4786(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 329.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + a 2,3-saturated acyl-CoA = a 2,3-dehydroacyl-CoA + AH2;
CC Xref=Rhea:RHEA:48608, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:60015, ChEBI:CHEBI:65111;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q2LQP0};
CC -!- DEVELOPMENTAL STAGE: Expressed in the mother cell at intermediate
CC stages of sporulation under the control of the sigma-E factor.
CC {ECO:0000269|PubMed:8759838}.
CC -!- INDUCTION: Subject to catabolite repression.
CC {ECO:0000269|PubMed:8759838}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U29084; AAB09615.1; -; Genomic_DNA.
DR EMBL; D84432; BAA12589.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14346.2; -; Genomic_DNA.
DR PIR; D69658; D69658.
DR RefSeq; NP_390295.2; NC_000964.3.
DR RefSeq; WP_003245999.1; NZ_JNCM01000036.1.
DR RefSeq; WP_009967692.1; NZ_CM000487.1.
DR PDB; 5LNX; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-379.
DR PDBsum; 5LNX; -.
DR AlphaFoldDB; P45857; -.
DR SMR; P45857; -.
DR STRING; 224308.BSU24150; -.
DR PaxDb; P45857; -.
DR PRIDE; P45857; -.
DR EnsemblBacteria; CAB14346; CAB14346; BSU_24150.
DR GeneID; 938664; -.
DR KEGG; bsu:BSU24150; -.
DR PATRIC; fig|224308.179.peg.2629; -.
DR eggNOG; COG1960; Bacteria.
DR InParanoid; P45857; -.
DR OMA; LYREAPM; -.
DR PhylomeDB; P45857; -.
DR BioCyc; BSUB:BSU24150-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
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.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Oxidoreductase; Reference proteome;
KW Sporulation.
FT CHAIN 1..379
FT /note="Acyl-CoA dehydrogenase"
FT /id="PRO_0000201183"
FT CONFLICT 97
FT /note="L -> M (in Ref. 1; AAB09615)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="A -> D (in Ref. 1; AAB09615)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="Missing (in Ref. 2; BAA12589)"
FT /evidence="ECO:0000305"
FT HELIX 7..32
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:5LNX"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:5LNX"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:5LNX"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5LNX"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:5LNX"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5LNX"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:5LNX"
FT STRAND 145..156
FT /evidence="ECO:0007829|PDB:5LNX"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:5LNX"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:5LNX"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:5LNX"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:5LNX"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:5LNX"
FT STRAND 207..218
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:5LNX"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 229..265
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 277..304
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 311..326
FT /evidence="ECO:0007829|PDB:5LNX"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 337..341
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 348..356
FT /evidence="ECO:0007829|PDB:5LNX"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:5LNX"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:5LNX"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:5LNX"
SQ SEQUENCE 379 AA; 40941 MW; 842FA980747D6C20 CRC64;
MHVTQEQVMM RKMVRDFARK EIAPAAEIME KTDEFPFQLI KKMGKHGLMG IPVPEQYGGA
GADVVSYILA IHEISRISAA VGVILSVHTS VGTNPILYFG NEEQKMKYIP NLASGDHLGA
FALTEPHSGS DAGSLRTTAI KKNGKYLLNG SKIFITNGGA ADIYITFALT APDQGRHGIS
AFIVEKNTPG FTVGKKERKL GLYGSNTTEL IFDNAEVPEA NLLGKEGDGF HIAMANLNVG
RIGIAAQALG IAEAALEHAV DYAKQRVQFG RPIAANQGIS FKLADMATRA EAARHLVYHA
ADLHNRGLNC GKEASMAKQF ASDAAVKAAL DAVQIYGGYG YMKDYPVERL LRDAKVTQIY
EGTNEIQRLI ISKYLLGGT
