BACC_BACSU
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 03-AUG-2022, entry version 134.
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 AlphaFoldDB; P39640; -.
DR SMR; P39640; -.
DR STRING; 224308.BSU37720; -.
DR PaxDb; P39640; -.
DR PRIDE; 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; PYDDFPE; -.
DR BioCyc; BSUB:BSU37720-MON; -.
DR BioCyc; MetaCyc:MON-19127; -.
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 ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 9..31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P16544"
FT BINDING 139
FT /ligand="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
