ID C2NCL1_BACCE Unreviewed; 353 AA.
AC C2NCL1;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=UDP-glucose 6-dehydrogenase {ECO:0000313|EMBL:EEK58218.1};
GN ORFNames=bcere0004_4100 {ECO:0000313|EMBL:EEK58218.1};
OS Bacillus cereus BGSC 6E1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=526970 {ECO:0000313|EMBL:EEK58218.1};
RN [1] {ECO:0000313|EMBL:EEK58218.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGSC 6E1 {ECO:0000313|EMBL:EEK58218.1};
RX PubMed=22645259; DOI=10.1101/gr.134437.111;
RA Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT "Genomic characterization of the Bacillus cereus sensu lato species:
RT Backdrop to the evolution of Bacillus anthracis.";
RL Genome Res. 22:1512-1524(2012).
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|PIRNR:PIRNR000124}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEK58218.1}.
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DR EMBL; ACLU01000018; EEK58218.1; -; Genomic_DNA.
DR AlphaFoldDB; C2NCL1; -.
DR HOGENOM; CLU_023810_3_2_9; -.
DR Proteomes; UP000000284; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; 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:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017476; UDP-Glc/GDP-Man.
DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf.
DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR InterPro; IPR028359; UDP_ManNAc/GlcNAc_DH.
DR NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR PANTHER; PTHR43491; UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE; 1.
DR PANTHER; PTHR43491:SF1; UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE; 1.
DR Pfam; PF00984; UDPG_MGDP_dh; 1.
DR Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR Pfam; PF03721; UDPG_MGDP_dh_N; 1.
DR PIRSF; PIRSF500136; UDP_ManNAc_DH; 1.
DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 256..350
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 353 AA; 39343 MW; 4E7EAEFBCBA38D56 CRC64;
MTKKKLIVNT PDQGIAEFQN SDYVIVTVPT PINEQREPDL SALISASHYI QQNLQKGQTF
IFESSTYPGT LEEVIIPIIS QTGKKAGEDF YIGYSPERID PANSQYSVQS IPKVISGQTE
KCKQKVQALY STIFDVVVPV SSPKVAEMCK LFENIQRLVN ISLVNELNTL CESLGIDFYE
ALEAASTKPF GFTPYWPGPG IGGHCIPVDP LYFQWRIKKN GAMSQLIEAA HVINEEMPEK
MVQKVKGVVQ PPATVLIVGI AYKKDVNDLR ESPALPIIEL LIKEGYEIEY HDPYISSAKF
GDKVYQSVSL NEQAVNQASC ILILTDHSNI DWKLFKGIKQ VVDTRGIVKK VSK
//
