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Database: UniProt
Entry: A0A261SDG1_9BORD
LinkDB: A0A261SDG1_9BORD
Original site: A0A261SDG1_9BORD 
ID   A0A261SDG1_9BORD        Unreviewed;       424 AA.
AC   A0A261SDG1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Vi polysaccharide biosynthesis protein VipA/TviB {ECO:0000313|EMBL:OZI35101.1};
GN   ORFNames=CAL29_14900 {ECO:0000313|EMBL:OZI35101.1};
OS   Bordetella genomosp. 10.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1416804 {ECO:0000313|EMBL:OZI35101.1, ECO:0000313|Proteomes:UP000216020};
RN   [1] {ECO:0000313|EMBL:OZI35101.1, ECO:0000313|Proteomes:UP000216020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU16122 {ECO:0000313|EMBL:OZI35101.1,
RC   ECO:0000313|Proteomes:UP000216020};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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:OZI35101.1}.
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DR   EMBL; NEVM01000002; OZI35101.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261SDG1; -.
DR   Proteomes; UP000216020; Unassembled WGS sequence.
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}.
FT   DOMAIN          317..417
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   424 AA;  46540 MW;  58D5EAF409A522A9 CRC64;
     MRLEDVKLGV VGLGYVGLPL AVEFGKKRPV IGFDIDTQRI RELKEGHDHT LEVAASELAE
     AAHLGYTDDR ETLGRANVFI VTVPTPIDAY KRPDLTPLVR ASETLGAVLK RGDVVIYEST
     VYPGATEEDC VPILERVSGL VFNRDFFVGY SPERINPGDK AHRVSTIKKV TSGSTPETAE
     LVDALYREII VAGTHKAASI RVAEAAKVIE NTQRDVNIAL VNELALIFNK MGIDTEAVLE
     AAGTKWNFLP FRPGLVGGHC IGVDPYYLTH KAQAIGYQPE IILAGRRLND GMGSYVVAQL
     VKAMTRRRIH VQGAKVLVLG LAFKENCPDL RNTRVADIIS ELAEYNVDVD VFDPWVDAAE
     ASAEYGVKLV SEPRNGDYDG IILAVAHAQF AEMGAERIRG FGRADHVLYD LKYVLKPHEA
     DLRL
//
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