ID Q7BQ74_BACCE Unreviewed; 282 AA.
AC Q7BQ74;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=3-hydroxybutyryl-CoA dehydrogenase {ECO:0000313|EMBL:QFY03527.1};
DE SubName: Full=ZmaG {ECO:0000313|EMBL:AAR87756.1};
GN Name=zmaG {ECO:0000313|EMBL:AAR87756.1};
GN ORFNames=GE376_30770 {ECO:0000313|EMBL:QFY03527.1};
OS Bacillus cereus.
OG Plasmid p1 {ECO:0000313|EMBL:QFY03527.1,
OG ECO:0000313|Proteomes:UP000326633}.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396 {ECO:0000313|EMBL:AAR87756.1};
RN [1] {ECO:0000313|EMBL:AAR87756.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UW85 {ECO:0000313|EMBL:AAR87756.1};
RX PubMed=8763956;
RA Milner J.L., Stohl E.A., Handelsman J.;
RT "Zwittermicin A resistance gene from Bacillus cereus.";
RL J. Bacteriol. 178:4266-4272(1996).
RN [2] {ECO:0000313|EMBL:AAR87756.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UW85 {ECO:0000313|EMBL:AAR87756.1};
RX PubMed=10521664; DOI=10.1016/S0378-1119(99)00315-7;
RA Stohl E.A., Milner J.L., Handelsman J.;
RT "Zwittermicin A biosynthetic cluster.";
RL Gene 237:403-411(1999).
RN [3] {ECO:0000313|EMBL:AAR87756.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UW85 {ECO:0000313|EMBL:AAR87756.1};
RA Emmert E.A.B., Klimowicz A.K., Thomas M.G., Handelsman J.;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AAR87756.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UW85 {ECO:0000313|EMBL:AAR87756.1};
RX PubMed=14711631; DOI=10.1128/AEM.70.1.104-113.2004;
RA Emmert E.A., Klimowicz A.K., Thomas M.G., Handelsman J.;
RT "Genetics of zwittermicin a production by Bacillus cereus.";
RL Appl. Environ. Microbiol. 70:104-113(2004).
RN [5] {ECO:0000313|EMBL:AAR87756.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UW85 {ECO:0000313|EMBL:AAR87756.1};
RA Kevany B.M., Rasko D.A., Thomas M.G.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:AAR87756.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UW85 {ECO:0000313|EMBL:AAR87756.1};
RX PubMed=19098220; DOI=10.1128/AEM.02518-08;
RA Kevany B.M., Rasko D.A., Thomas M.G.;
RT "Characterization of the complete zwittermicin A biosynthesis gene cluster
RT from Bacillus cereus.";
RL Appl. Environ. Microbiol. 75:1144-1155(2009).
RN [7] {ECO:0000313|EMBL:QFY03527.1, ECO:0000313|Proteomes:UP000326633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB1 {ECO:0000313|EMBL:QFY03527.1,
RC ECO:0000313|Proteomes:UP000326633};
RC PLASMID=p1 {ECO:0000313|EMBL:QFY03527.1,
RC ECO:0000313|Proteomes:UP000326633};
RA Batinovic S., Petrovski S.;
RT "Bacillus cereus SB1 complete genome.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FJ430564; AAR87756.1; -; Genomic_DNA.
DR EMBL; CP045607; QFY03527.1; -; Genomic_DNA.
DR RefSeq; WP_000473350.1; NZ_NVDN01000009.1.
DR AlphaFoldDB; Q7BQ74; -.
DR SMR; Q7BQ74; -.
DR GeneID; 67469887; -.
DR PATRIC; fig|1396.545.peg.6078; -.
DR BioCyc; MetaCyc:MONOMER-19432; -.
DR Proteomes; UP000326633; Plasmid p1.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR022694; 3-OHacyl-CoA_DH.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR48075:SF7; 3-HYDROXYACYL-COA DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR PIRSF; PIRSF000105; HCDH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW NAD {ECO:0000256|PIRSR:PIRSR000105-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Plasmid {ECO:0000313|EMBL:QFY03527.1}.
FT DOMAIN 4..183
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 186..282
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT BINDING 9..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 92
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT SITE 140
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ SEQUENCE 282 AA; 31625 MW; E716D7D9ACA7785C CRC64;
MFKKIGIVGA GTMGIGMAVD LVLHGLETVL IDVTEEQLEK AEEKILETVR FAPLINKAFP
RMHKEEVLSL ISSSTNLDEV AECDYIVENV PENWQIKEPI YRRLDEICKK DTIFGVNTSC
ISITKVGGVT KRPDKIIGMH FMNPVYMKPS IEVIRGHLTS DETVEKAQSF LKQLDKDAIV
VNDQTGFVSN RISHLFMNES AWVVMDGVAT PKQVDDIFKK CFGHTMGPLE TADLIGLDTV
LHSLNVLYEE YQDPKFRCCP LLKKMVDAGE CGRKSGKGFY AY
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