BIOW_BACSU
ID BIOW_BACSU Reviewed; 259 AA.
AC P53559;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=6-carboxyhexanoate--CoA ligase;
DE EC=6.2.1.14;
DE AltName: Full=Pimeloyl-CoA synthase;
GN Name=bioW; OrderedLocusNames=BSU30240;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8763940; DOI=10.1128/jb.178.14.4122-4130.1996;
RA Bower S., Perkins J.B., Yocum R.R., Howitt C.L., Rahaim P., Pero J.;
RT "Cloning, sequencing, and characterization of the Bacillus subtilis biotin
RT biosynthetic operon.";
RL J. Bacteriol. 178:4122-4130(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
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).
CC -!- FUNCTION: Catalyzes the transformation of pimelate into pimeloyl-CoA
CC with concomitant hydrolysis of ATP to AMP. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + heptanedioate = 6-carboxyhexanoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:14781, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:36165, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57360, ChEBI:CHEBI:456215; EC=6.2.1.14;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Metabolic intermediate metabolism; pimeloyl-CoA biosynthesis;
CC pimeloyl-CoA from pimelate: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BioW family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC00261.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB15002.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U51868; AAB17457.1; -; Genomic_DNA.
DR EMBL; AF008220; AAC00261.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB15002.3; ALT_INIT; Genomic_DNA.
DR PIR; H69594; H69594.
DR RefSeq; NP_390902.3; NC_000964.3.
DR PDB; 5FLG; X-ray; 2.04 A; A/B=4-259.
DR PDB; 5FLL; X-ray; 2.34 A; A/B=4-259.
DR PDB; 5FM0; X-ray; 2.44 A; A/B=4-259.
DR PDB; 5G1F; X-ray; 2.25 A; A/B=4-259.
DR PDBsum; 5FLG; -.
DR PDBsum; 5FLL; -.
DR PDBsum; 5FM0; -.
DR PDBsum; 5G1F; -.
DR AlphaFoldDB; P53559; -.
DR SMR; P53559; -.
DR STRING; 224308.BSU30240; -.
DR SwissLipids; SLP:000001730; -.
DR PaxDb; P53559; -.
DR PRIDE; P53559; -.
DR EnsemblBacteria; CAB15002; CAB15002; BSU_30240.
DR GeneID; 938017; -.
DR KEGG; bsu:BSU30240; -.
DR PATRIC; fig|224308.43.peg.3163; -.
DR eggNOG; COG1424; Bacteria.
DR InParanoid; P53559; -.
DR BioCyc; BSUB:BSU30240-MON; -.
DR BioCyc; MetaCyc:BSU30240-MON; -.
DR BRENDA; 6.2.1.14; 658.
DR UniPathway; UPA00999; UER00351.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0042410; F:6-carboxyhexanoate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00668; BioW; 1.
DR InterPro; IPR005499; BioW.
DR Pfam; PF03744; BioW; 1.
DR TIGRFAMs; TIGR01204; bioW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Biotin biosynthesis; Ligase; Magnesium;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..259
FT /note="6-carboxyhexanoate--CoA ligase"
FT /id="PRO_0000191016"
FT STRAND 7..17
FT /evidence="ECO:0007829|PDB:5FLG"
FT STRAND 25..35
FT /evidence="ECO:0007829|PDB:5FLG"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5FLG"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:5FLG"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:5FLG"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5FLG"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:5FLG"
FT HELIX 88..101
FT /evidence="ECO:0007829|PDB:5FLG"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:5FLG"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:5FLG"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:5FLG"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:5FLG"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:5FLG"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:5FLG"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:5FLG"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:5FLG"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:5FLG"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:5FLG"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:5FLG"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:5FLG"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:5FLG"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:5FLG"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:5FLG"
SQ SEQUENCE 259 AA; 29630 MW; 3820F43A33DDE2CE CRC64;
MMQEETFYSV RMRASMNGSH EDGGKHISGG ERLIPFHEMK HTVNALLEKG LSHSRGKPDF
MQIQFEEVHE SIKTIQPLPV HTNEVSCPEE GQKLARLLLE KEGVSRDVIE KAYEQIPEWS
DVRGAVLFDI HTGKRMDQTK EKGVRVSRMD WPDANFEKWA LHSHVPAHSR IKEALALASK
VSRHPAVVAE LCWSDDPDYI TGYVAGKKMG YQRITAMKEY GTEEGCRVFF IDGSNDVNTY
IHDLEKQPIL IEWEEDHDS
