P44914 (RMLB_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
dTDP-glucose 4,6-dehydratase
EC=4.2.1.46

Gene names

Name:	rffG
Ordered Locus Names:	HI_0873

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction By similarity.
Catalytic activity	dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O.
Cofactor	Binds 1 NAD ion per monomer By similarity.
Pathway	Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis. Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the sugar epimerase family. dTDP-glucose dehydratase subfamily.

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Ligand	NAD
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	O antigen biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway dTDP-rhamnose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway extracellular polysaccharide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB lipopolysaccharide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	coenzyme binding Inferred from electronic annotation. Source: InterPro dTDP-glucose 4,6-dehydratase activity Inferred from sequence or structural similarity. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 338	338	dTDP-glucose 4,6-dehydratase		PRO_0000183237
Regions
	Nucleotide binding	8 – 14	7	NAD Potential
	Nucleotide binding	33 – 36	4	NAD By similarity
	Nucleotide binding	59 – 60	2	NAD By similarity
	Nucleotide binding	160 – 164	5	NAD By similarity
	Region	134 – 136	3	Substrate binding By similarity
	Region	199 – 200	2	Substrate binding By similarity
	Region	215 – 217	3	Substrate binding By similarity
	Region	294 – 297	4	Substrate binding By similarity
Sites
	Active site	135	1	Proton donor By similarity
	Active site	136	1	Proton acceptor By similarity
	Active site	160	1	Proton acceptor By similarity
	Binding site	81	1	NAD; via carbonyl oxygen By similarity
	Binding site	85	1	Substrate; via carbonyl oxygen By similarity
	Binding site	100	1	NAD By similarity
	Binding site	189	1	Substrate By similarity
	Binding site	190	1	NAD; via amide nitrogen By similarity
	Binding site	224	1	Substrate By similarity
	Binding site	259	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P44914 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: B44BCC29D6C7D04B	FASTA	338	38,329
	10 20 30 40 50 60 MMNILVTGGS GFIGSALIRY IINHTQDFVI NIDKLTYAAN QSALREVENN PRYVFEKVDI 70 80 90 100 110 120 CDLNVIENIF EKYQPDAVMH LAAESHVDRS ISGAADFVQT NIVGTYTLLE VAKNYWHTLD 130 140 150 160 170 180 EAKKTTFRFH HISTDEVYGD LSLSEPAFTE QSPYHPSSPY SASKAASNHL VQAWHRTYGL 190 200 210 220 230 240 PVIITNSSNN YGAYQHAEKL IPLMISNAVM GKPLPIYGDG QQIRDWLFVE DHVQASYLVL 250 260 270 280 290 300 TKGRVGENYN IGGNCEKTNL EVVKRICQLL EELAPSKPNH IKYYEDLMTF VKDRPGHDVR 310 320 330 YSLDCSKIHA ELGWQPQITF EQGLRQTVKW YLFNSSSS

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22531.1.
PIR	C64099.
RefSeq	NP_439034.2. NC_000907.1.
3D structure databases
ProteinModelPortal	P44914.
SMR	P44914. Positions 1-336.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI0873.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC22531; AAC22531; HI_0873.
GeneID	949510.
KEGG	hin:HI0873.
PATRIC	20190401. VBIHaeInf48452_0914.
Phylogenomic databases
eggNOG	COG1088.
KO	K01710.
OMA	AKKAFRF.
ProtClustDB	CLSK824762.
Enzyme and pathway databases
UniPathway	UPA00124. UPA00281.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR005888. dTDP_Gluc_deHydtase. IPR001509. Epimerase_deHydtase. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR10366:SF41. PTHR10366:SF41. 1 hit.
Pfam	PF01370. Epimerase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01181. dTDP_gluc_dehyt. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RMLB_HAEIN

Accession

Primary (citable) accession number: P44914

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program