ID A0A0S4LC98_9BACT Unreviewed; 359 AA.
AC A0A0S4LC98;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=dTDP-glucose 4,6-dehydratase {ECO:0000256|ARBA:ARBA00011990, ECO:0000256|RuleBase:RU004473};
DE EC=4.2.1.46 {ECO:0000256|ARBA:ARBA00011990, ECO:0000256|RuleBase:RU004473};
GN Name=rmlB {ECO:0000313|EMBL:CUS35125.1};
GN ORFNames=COMA1_20133 {ECO:0000313|EMBL:CUS35125.1};
OS Candidatus Nitrospira nitrosa.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1742972 {ECO:0000313|EMBL:CUS35125.1, ECO:0000313|Proteomes:UP000199032};
RN [1] {ECO:0000313|EMBL:CUS35125.1, ECO:0000313|Proteomes:UP000199032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COMA1 {ECO:0000313|EMBL:CUS35125.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose
CC + H2O; Xref=Rhea:RHEA:17221, ChEBI:CHEBI:15377, ChEBI:CHEBI:57477,
CC ChEBI:CHEBI:57649; EC=4.2.1.46;
CC Evidence={ECO:0000256|ARBA:ARBA00001539,
CC ECO:0000256|RuleBase:RU004473};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911,
CC ECO:0000256|RuleBase:RU004473};
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. dTDP-glucose dehydratase subfamily.
CC {ECO:0000256|ARBA:ARBA00008178, ECO:0000256|RuleBase:RU004473}.
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DR EMBL; CZQA01000008; CUS35125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4LC98; -.
DR STRING; 1742972.COMA1_20133; -.
DR OrthoDB; 9803010at2; -.
DR Proteomes; UP000199032; Unassembled WGS sequence.
DR GO; GO:0008460; F:dTDP-glucose 4,6-dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0009225; P:nucleotide-sugar metabolic process; IEA:InterPro.
DR CDD; cd05246; dTDP_GD_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR InterPro; IPR005888; dTDP_Gluc_deHydtase.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01181; dTDP_gluc_dehyt; 1.
DR PANTHER; PTHR43000; DTDP-D-GLUCOSE 4,6-DEHYDRATASE-RELATED; 1.
DR PANTHER; PTHR43000:SF47; DTDP-GLUCOSE 4,6-DEHYDRATASE 2; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU004473, ECO:0000313|EMBL:CUS35125.1};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000199032}.
FT DOMAIN 4..328
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 359 AA; 39787 MW; A72375D43FFE6224 CRC64;
MSILVTGGAG FIGANFVLDW LTQHDESVVN LDKLTYAGNL ESLVSLGNDE RHIFVRGDIG
DAALVDKLLK EHGPRAVINF AAESHVDRSI HGPGEFIQTN IVGTFHLLES VRAYWGALAG
EAKQRFRFLH VSTDEVYGSL THDAPAFSEM NRYEPNSPYS ASKAASDHLV RAYHHTYGLP
VLTTNCSNNY GPYQFPEKLI PLCILNALAG KPLPIYGDGL QVRDWLYVND HCRAISLVLQ
GGLVGETYNI GGWNEKTNLD VVQTLCDTLD GLAPPATCHL PPATCRSLIT FVKDRPGHDR
RYAMDASKIE RELGWKPLET FESGLRKTVT WYLQNPRWIA NVTSGAYRTW IDQQYGAGA
//
