ID A0A0Q9PX90_9GAMM Unreviewed; 426 AA.
AC A0A0Q9PX90;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Vi polysaccharide biosynthesis protein VipA/TviB {ECO:0000313|EMBL:KRE91161.1};
GN ORFNames=ASG87_18595 {ECO:0000313|EMBL:KRE91161.1};
OS Frateuria sp. Soil773.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Frateuria.
OX NCBI_TaxID=1736407 {ECO:0000313|EMBL:KRE91161.1, ECO:0000313|Proteomes:UP000051919};
RN [1] {ECO:0000313|Proteomes:UP000051919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil773 {ECO:0000313|Proteomes:UP000051919};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE91161.1, ECO:0000313|Proteomes:UP000051919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil773 {ECO:0000313|EMBL:KRE91161.1,
RC ECO:0000313|Proteomes:UP000051919};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE91161.1}.
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DR EMBL; LMSL01000033; KRE91161.1; -; Genomic_DNA.
DR RefSeq; WP_056004496.1; NZ_LMSL01000033.1.
DR AlphaFoldDB; A0A0Q9PX90; -.
DR STRING; 1736407.ASG87_18595; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000051919; 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 318..419
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 426 AA; 46379 MW; 0F553E6EF829E86F CRC64;
MQNLESTKIA IVGLGYVGLP LAVEFGKRFD TLGFDINAAR IEQLRKGDDH TRETSAEELK
QATRLNFATD IAEIKGCTVF IVTVPTPVDE HKRPDFTPLI KASQAIGGVL NRGDVVIYES
TVYPGATEEI CVPELERVSG LRFNADFTVG YSPERINPGD KQRRLTTIPK ITSGSTPETA
DFVDALYGRI IAAGTHKAPS IKVAEAAKVI ENTQRDANIA LINEFALIFH RLGIDTSDVL
AAAGTKWNFL PFQPGLVGGH CIGVDPYYLI QKAQAVGYYP DILLACRRIN DAMGQHVASE
VVKLMIGKGH AIKGSRVLVL GLTFKENCPD LRNTRVVDLV REFESYGAVV DVYDPWVDVV
EAEAEYGLKP LGEAPRPGTY DAVVLAVAHD EFKSAGSEAV RTWANGRAVL YDIKGVLPKD
AVDGRL
//
