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Database: UniProt
Entry: I0JRN8_HALH3
LinkDB: I0JRN8_HALH3
Original site: I0JRN8_HALH3 
ID   I0JRN8_HALH3            Unreviewed;       425 AA.
AC   I0JRN8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=UDP-glucose/GDP-mannose dehydrogenase {ECO:0000313|EMBL:CCG46809.1};
GN   OrderedLocusNames=HBHAL_4469 {ECO:0000313|EMBL:CCG46809.1};
OS   Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS   3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=866895 {ECO:0000313|EMBL:CCG46809.1, ECO:0000313|Proteomes:UP000007397};
RN   [1] {ECO:0000313|EMBL:CCG46809.1, ECO:0000313|Proteomes:UP000007397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 /
RC   NBRC 102448 / NCIMB 2269 {ECO:0000313|Proteomes:UP000007397};
RX   PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA   Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA   Oesterhelt D.;
RT   "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT   salinities by the moderately halophilic, chloride-dependent bacterium
RT   Halobacillus halophilus.";
RL   Environ. Microbiol. 15:1619-1633(2013).
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR   EMBL; HE717023; CCG46809.1; -; Genomic_DNA.
DR   RefSeq; WP_014644694.1; NC_017668.1.
DR   AlphaFoldDB; I0JRN8; -.
DR   STRING; 866895.HBHAL_4469; -.
DR   KEGG; hhd:HBHAL_4469; -.
DR   PATRIC; fig|866895.3.peg.3503; -.
DR   eggNOG; COG0677; Bacteria.
DR   HOGENOM; CLU_023810_3_2_9; -.
DR   Proteomes; UP000007397; 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:SF2; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007397}.
FT   DOMAIN          310..406
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   425 AA;  47016 MW;  70B705B066A86E5A CRC64;
     MKKSLCVVGL GYIGLPTSVM FAINGHQVHG VDVNRKAVEM VNAKQLHIEE NGLQERLEEA
     VDSGKFTASL EPTEADVFVI AVPSPIREDK TANLDYVKKA TESIVPFVKE GNLVILESTV
     PPRTVEDVML PVLEETGLTI GEELFVSHSP ERVIPGKVFQ ELVDNDRIVG GINEKSSEMT
     RDLYLSFVKG NIHLTDATTA EMAKVIENTY RDVNIAFANE LALISDQIGV NSWEAIKLAN
     YHPRVNIHTP GPGVGGHCIA VDPWFLAEIQ PDLSKIIQLS RNTNDHMPVY TAGEVESFLK
     EQHIQDPKVA LFGLSFKANI DDQRESPSLK VILELVERGI SFSSYDPHIK ENVASNQTQS
     MDEALEGADI VVILTDHDEF KQLDPAHIQG KMRSRLVFDT KNALSLDEWK DAGFLTKRLG
     DSKNG
//
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