ID E3HF56_ACHXA Unreviewed; 425 AA.
AC E3HF56;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Vi polysaccharide biosynthesis protein VipA/TviB {ECO:0000313|EMBL:ADP18915.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:ADP18915.1};
GN Name=vipA {ECO:0000313|EMBL:ADP18915.1};
GN OrderedLocusNames=AXYL_05616 {ECO:0000313|EMBL:ADP18915.1};
OS Achromobacter xylosoxidans (strain A8).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP18915.1, ECO:0000313|Proteomes:UP000006876};
RN [1] {ECO:0000313|EMBL:ADP18915.1, ECO:0000313|Proteomes:UP000006876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A8 {ECO:0000313|EMBL:ADP18915.1,
RC ECO:0000313|Proteomes:UP000006876};
RX PubMed=21097610; DOI=10.1128/JB.01299-10;
RA Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT Achromobacter xylosoxidans A8.";
RL J. Bacteriol. 193:791-792(2011).
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR EMBL; CP002287; ADP18915.1; -; Genomic_DNA.
DR RefSeq; WP_013396214.1; NC_014640.1.
DR AlphaFoldDB; E3HF56; -.
DR STRING; 762376.AXYL_05616; -.
DR KEGG; axy:AXYL_05616; -.
DR PATRIC; fig|762376.5.peg.5623; -.
DR eggNOG; COG0677; Bacteria.
DR HOGENOM; CLU_023810_3_1_4; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000006876; 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 ECO:0000313|EMBL:ADP18915.1}.
FT DOMAIN 318..418
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 425 AA; 46800 MW; 7FA3699ECE7E6657 CRC64;
MLRIQDVKLA VVGLGYVGLP LAVEFGKKRS VIGFDINTRR IDALKAGHDH TLEVSDEELK
EATQLSYTAD RAVLGQANVY IVTVPTPIDE YKQPDLTPLV KASETIGAVL KRGDIVIYES
TVYPGATEED CVPVLERVSG LKFNVDFYAG YSPERINPGD KAHRVSTIKK VTSGSTPEVA
ELVDQLYQQI IVAGTHKASS IRVAEAAKVI ENTQRDVNIA LINELALIFN KMGIDTEAVL
QAAGTKWNFL PFRPGLVGGH CIGVDPYYLT HKAQSIGYHP EIILAGRRLN DSMGGYVVSQ
LVKAMTKRRI HVQGARVLVM GLAFKENCPD LRNTRIVDIV KELGDYNVAV DVYDPWVDPE
EAVHEYGITP VANLEEGKYD AVILGVAHHQ FTEMGATGIR KLGKPEHILY DLKYVLSPDE
SDLRL
//
