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O34354 (UXAB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Altronate oxidoreductase

EC=1.1.1.58
Alternative name(s):
Tagaturonate dehydrogenase
Tagaturonate reductase
Gene names
Name:uxaB
Synonyms:yjmI
Ordered Locus Names:BSU12380
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

D-altronate + NAD+ = D-tagaturonate + NADH. HAMAP-Rule MF_00670

Pathway

Carbohydrate metabolism; pentose and glucuronate interconversion. HAMAP-Rule MF_00670

Induction

Induced by galacturonate, repressed by glucose Probable. Ref.3

Miscellaneous

Member of the exu locus which is required for galacturonate utilization.

Sequence similarities

Belongs to the mannitol dehydrogenase family. UxaB subfamily.

Ontologies

Keywords
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functioncoenzyme binding

Inferred from electronic annotation. Source: InterPro

tagaturonate reductase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Altronate oxidoreductase HAMAP-Rule MF_00670
PRO_0000170739

Regions

Nucleotide binding19 – 3012NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
O34354 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: DC7DBC8DA500F8D4

FASTA48055,361
        10         20         30         40         50         60 
MQKLNKNVYD HYTQYPEKIL QFGEGNFLRG FIDWQIDQLN QHTDFNGSVA VVQPRGSEKI 

        70         80         90        100        110        120 
KRLNEQDGLY TLFLQGMKDG EAVNEHMIIN SISRGIDLFS DYEAYKELAS SERLRFIISN 

       130        140        150        160        170        180 
TTEAGIVCDE KDRLEDRPQK TFPGKLTAFL YFRYQAFKGD QTKGCVLIPC ELIENNGEKL 

       190        200        210        220        230        240 
RETVLHYAHL WKLEEGFTQW IHEANTFCNS LVDRIVPGFP VDSIDEITAD LGYQDDLIVV 

       250        260        270        280        290        300 
GEQYYLWVIE GPDWIGKELP FAAAGLHTKI VSDLTPYRTK KVRILNGAHT AMTPVALLYG 

       310        320        330        340        350        360 
LKTVRDAVEH PEVGRFIREL IDDEILPVLK MEGLSQYADD VLNRFKNPYI KHYLESIALN 

       370        380        390        400        410        420 
AISKFKTRNL PTLKEYAEQK GQLPERLVFS FSALLYFYHD NETLQDDPAV LQFFKEVWCQ 

       430        440        450        460        470        480 
EDGDMLRIAS RVLGEQRLWG ADLNEIPKLT DRVAVYLNHI HELGMQRALE QYCIQGGEVR 

« Hide

References

« Hide 'large scale' references
[1]"A 35.7 kb DNA fragment from the Bacillus subtilis chromosome containing a putative 12.3 kb operon involved in hexuronate catabolism and a perfectly symmetrical hypothetical catabolite-responsive element."
Rivolta C., Soldo B., Lazarevic V., Joris B., Mauel C., Karamata D.
Microbiology 144:877-884(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROBABLE OPERON STRUCTURE.
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Regulation of hexuronate utilization in Bacillus subtilis."
Mekjian K.R., Bryan E.M., Beall B.W., Moran C.P. Jr.
J. Bacteriol. 181:426-433(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROBABLE OPERON STRUCTURE, INDUCTION.
Strain: 168 / MB24.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF015825 Genomic DNA. Translation: AAC46334.1.
AL009126 Genomic DNA. Translation: CAB13095.1.
PIRC69853.
RefSeqNP_389120.1. NC_000964.3.

3D structure databases

ProteinModelPortalO34354.
SMRO34354. Positions 3-474.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU12380.

Proteomic databases

PaxDbO34354.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13095; CAB13095; BSU12380.
GeneID936468.
KEGGbsu:BSU12380.
PATRIC18974217. VBIBacSub10457_1301.

Organism-specific databases

GenoListBSU12380. [Micado]

Phylogenomic databases

eggNOGCOG0246.
HOGENOMHOG000029586.
KOK00041.
OMARVIQFGE.
OrthoDBEOG6CVVB8.
ProtClustDBPRK03643.

Enzyme and pathway databases

BioCycBSUB:BSU12380-MONOMER.
UniPathwayUPA00246.

Family and domain databases

Gene3D1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPMF_00670. Altron_oxidoreduct.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR023668. Altronate_OxRdtase.
IPR013328. DH_multihelical.
IPR000669. Mannitol_DH.
IPR013118. Mannitol_DH_C.
IPR013131. Mannitol_DH_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01232. Mannitol_dh. 1 hit.
PF08125. Mannitol_dh_C. 1 hit.
[Graphical view]
PRINTSPR00084. MTLDHDRGNASE.
SUPFAMSSF48179. SSF48179. 1 hit.
ProtoNetSearch...

Entry information

Entry nameUXAB_BACSU
AccessionPrimary (citable) accession number: O34354
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: January 1, 1998
Last modified: February 19, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList