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Database: UniProt
Entry: P39640
LinkDB: P39640
Original site: P39640 
ID   BACC_BACSU              Reviewed;         253 AA.
AC   P39640;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   23-FEB-2022, entry version 132.
DE   RecName: Full=Dihydroanticapsin 7-dehydrogenase {ECO:0000303|PubMed:23317005};
DE            EC=1.1.1.385 {ECO:0000269|PubMed:23317005};
DE   AltName: Full=Bacilysin biosynthesis oxidoreductase BacC {ECO:0000303|PubMed:15609023};
GN   Name=bacC {ECO:0000303|PubMed:15609023}; Synonyms=ywfD;
GN   OrderedLocusNames=BSU37720; ORFNames=ipa-82d;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA   Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA   Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA   Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT   "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT   region from 325 degrees to 333 degrees.";
RL   Mol. Microbiol. 10:371-384(1993).
RN   [2]
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   [3]
RP   INDUCTION.
RC   STRAIN=168 / 61884;
RX   PubMed=12372825; DOI=10.1074/jbc.m208722200;
RA   Inaoka T., Takahashi K., Ohnishi-Kameyama M., Yoshida M., Ochi K.;
RT   "Guanine nucleotides guanosine 5'-diphosphate 3'-diphosphate and GTP co-
RT   operatively regulate the production of an antibiotic bacilysin in Bacillus
RT   subtilis.";
RL   J. Biol. Chem. 278:2169-2176(2003).
RN   [4]
RP   FUNCTION IN BACILYSIN PRODUCTION, AND GENE NAME.
RX   PubMed=15609023; DOI=10.1007/s00203-004-0743-8;
RA   Steinborn G., Hajirezaei M.-R., Hofemeister J.;
RT   "bac genes for recombinant bacilysin and anticapsin production in Bacillus
RT   host strains.";
RL   Arch. Microbiol. 183:71-79(2005).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, PATHWAY, AND SUBSTRATE
RP   SPECIFICITY.
RC   STRAIN=168;
RX   PubMed=23317005; DOI=10.1021/bi3016229;
RA   Parker J.B., Walsh C.T.;
RT   "Action and timing of BacC and BacD in the late stages of biosynthesis of
RT   the dipeptide antibiotic bacilysin.";
RL   Biochemistry 52:889-901(2013).
CC   -!- FUNCTION: Part of the bacABCDEFG operon responsible for the
CC       biosynthesis of bacilysin, an irreversible inactivator of the
CC       glutaminase domain of glucosamine synthetase. Catalyzes the
CC       dehydrogenation of the C7-hydroxyl group in the 4S-tetrahydrotyrosine
CC       (4S-H4Tyr) to yield anticapsin (epoxycyclohexanonyl-Ala). It is not
CC       able to oxidize the 4R-H4Tyr diastereomer and the dihydrobacilysin
CC       dipeptide (L-Ala-4S-H4Tyr dipeptide). {ECO:0000269|PubMed:15609023,
CC       ECO:0000269|PubMed:23317005}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-dihydroanticapsin + NAD(+) = H(+) + L-anticapsin + NADH;
CC         Xref=Rhea:RHEA:44628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:84310, ChEBI:CHEBI:84358;
CC         EC=1.1.1.385; Evidence={ECO:0000269|PubMed:23317005};
CC   -!- PATHWAY: Antibiotic biosynthesis; bacilysin biosynthesis.
CC       {ECO:0000305|PubMed:23317005}.
CC   -!- INDUCTION: The compound guanosine 5'-diphosphate 3'-diphosphate (ppGpp)
CC       is essential for the transcription of the bacABCDE operon and GTP
CC       regulates the transcription of both this operon and ywfH via the CodY-
CC       mediated regulation system. {ECO:0000269|PubMed:12372825}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show an accumulation of
CC       dihydroanticapsin and dihydrobacilysin. {ECO:0000269|PubMed:23317005}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA51638.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X73124; CAA51638.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB15799.2; -; Genomic_DNA.
DR   PIR; S39737; S39737.
DR   RefSeq; NP_391652.1; NC_000964.3.
DR   RefSeq; WP_003243359.1; NZ_JNCM01000034.1.
DR   PDB; 5ITV; X-ray; 2.26 A; A/B/C/D=1-253.
DR   PDB; 5ITW; X-ray; 1.19 A; A/B/C/D=1-253.
DR   PDBsum; 5ITV; -.
DR   PDBsum; 5ITW; -.
DR   SMR; P39640; -.
DR   STRING; 224308.BSU37720; -.
DR   PaxDb; P39640; -.
DR   EnsemblBacteria; CAB15799; CAB15799; BSU_37720.
DR   GeneID; 937065; -.
DR   KEGG; bsu:BSU37720; -.
DR   PATRIC; fig|224308.179.peg.4084; -.
DR   eggNOG; COG1028; Bacteria.
DR   InParanoid; P39640; -.
DR   OMA; AGVIHMS; -.
DR   BioCyc; BSUB:BSU37720-MONOMER; -.
DR   BRENDA; 1.1.1.385; 658.
DR   UniPathway; UPA00100; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic biosynthesis; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..253
FT                   /note="Dihydroanticapsin 7-dehydrogenase"
FT                   /id="PRO_0000054522"
FT   NP_BIND         9..31
FT                   /note="NAD"
FT                   /evidence="ECO:0000250|UniProtKB:P16544"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         139
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P16544"
FT   STRAND          7..11
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   TURN            12..14
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   HELIX           16..27
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   STRAND          31..37
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   HELIX           39..49
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   STRAND          54..58
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   HELIX           64..78
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   STRAND          83..86
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   HELIX           101..111
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   HELIX           113..129
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   STRAND          132..137
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   HELIX           140..142
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   HELIX           150..170
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   HELIX           171..173
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   STRAND          175..182
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   HELIX           188..197
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   STRAND          198..200
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   HELIX           202..210
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   HELIX           221..232
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   HELIX           234..236
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   STRAND          243..247
FT                   /evidence="ECO:0007829|PDB:5ITW"
FT   HELIX           250..252
FT                   /evidence="ECO:0007829|PDB:5ITW"
SQ   SEQUENCE   253 AA;  27080 MW;  20900690BFABB3A2 CRC64;
     MNLTDKTVLI TGGASGIGYA AVQAFLGQQA NVVVADIDEA QGEAMVRKEN NDRLHFVQTD
     ITDEAACQHA VESAVHTFGG LDVLINNAGI EIVAPIHEME LSDWNKVLQV NLTGMFLMSK
     HALKHMLAAG KGNIINTCSV GGLVAWPDIP AYNASKGGVL QLTKSMAVDY AKHQIRVNCV
     CPGIIDTPLN EKSFLENNEG TLEEIKKEKA KVNPLLRLGK PEEIANVMLF LASDLSSYMT
     GSAITADGGY TAQ
//
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