ID A0A0Q7SX54_9BACL Unreviewed; 455 AA.
AC A0A0Q7SX54;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=UDP-N-acetyl-D-glucosamine dehydrogenase {ECO:0000313|EMBL:KQY87598.1};
GN ORFNames=ASD24_07060 {ECO:0000313|EMBL:KQY87598.1};
OS Paenibacillus sp. Root52.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736552 {ECO:0000313|EMBL:KQY87598.1, ECO:0000313|Proteomes:UP000051734};
RN [1] {ECO:0000313|Proteomes:UP000051734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root52 {ECO:0000313|Proteomes:UP000051734};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY87598.1, ECO:0000313|Proteomes:UP000051734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root52 {ECO:0000313|EMBL:KQY87598.1,
RC ECO:0000313|Proteomes:UP000051734};
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:KQY87598.1}.
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DR EMBL; LMFO01000012; KQY87598.1; -; Genomic_DNA.
DR RefSeq; WP_056696409.1; NZ_LMFO01000012.1.
DR AlphaFoldDB; A0A0Q7SX54; -.
DR STRING; 1736552.ASD24_07060; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000051734; 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: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 333..429
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 455 AA; 51028 MW; 5D4F21390067B8C8 CRC64;
MHNQHFHSLL NAIENKEAVL GVVGLGYVGL PLAVEMVNQG FTVIGIDLDA SKVESIYHGD
SYIHDISSEE LKKVMETGRF QPTTDYSMLR VIDALSICVP TPLSENQDPD TSYIETVVDQ
IKLHMKPGML ITLESTTYPG TTEELIQQKL DKIGHEAGKD YFLCFSPERV DPSNGRFTTF
NTPKVIGGTT ESCLKLGTAL YGKYVQTVVP VSSPKVAEMS KLLENTFRSV NIAFVNEMAM
MCDRMGIDIW EVIDAAATKP FGFMPFYPGP GIGGHCIPLD PMYLSWKAKG FRFYSKFIEL
AQSTNDNMPY YVLNKTSTIL NEYAKSVRNS NILLLGMSYK PNIADLRESP GLEVYELFKE
SGANVSYYDP YADSFLDKHG DTVHSEVFNL EQFKTYDCIV LITNHKDLPY REISELGVPI
LDTRNAFRTY TQPHIYKIGH SVQHPVLEPS EALLV
//
