Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

L-rhamnose isomerase

Gene

L-RhI

Organism
Pseudomonas stutzeri (Pseudomonas perfectomarina)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi219 – 2191Copper 1Combined sources
Metal bindingi219 – 2191Manganese 1Combined sources
Metal bindingi219 – 2191Zinc 1Combined sources
Metal bindingi254 – 2541Copper 1Combined sources
Metal bindingi254 – 2541Manganese 1Combined sources
Metal bindingi254 – 2541Zinc 1Combined sources
Metal bindingi257 – 2571Copper 2; via tele nitrogenCombined sources
Metal bindingi257 – 2571Copper 3; via tele nitrogenCombined sources
Metal bindingi257 – 2571Manganese 2; via tele nitrogenCombined sources
Metal bindingi257 – 2571Manganese 3; via tele nitrogenCombined sources
Metal bindingi257 – 2571Zinc 2; via tele nitrogenCombined sources
Metal bindingi281 – 2811Copper 1; via pros nitrogenCombined sources
Metal bindingi281 – 2811Manganese 1; via pros nitrogenCombined sources
Metal bindingi281 – 2811Zinc 1; via pros nitrogenCombined sources
Metal bindingi289 – 2891Copper 2Combined sources
Metal bindingi289 – 2891Copper 3Combined sources
Metal bindingi289 – 2891Manganese 2Combined sources
Metal bindingi289 – 2891Manganese 3Combined sources
Metal bindingi289 – 2891Zinc 2Combined sources
Metal bindingi291 – 2911Copper 2Combined sources
Metal bindingi291 – 2911Copper 3Combined sources
Metal bindingi291 – 2911Manganese 2Combined sources
Metal bindingi291 – 2911Manganese 3Combined sources
Metal bindingi291 – 2911Zinc 2Combined sources
Metal bindingi298 – 2981Manganese 1Combined sources
Metal bindingi327 – 3271Copper 1Combined sources
Metal bindingi327 – 3271Manganese 1Combined sources
Metal bindingi327 – 3271Zinc 1Combined sources

GO - Molecular functioni

  1. isomerase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

IsomeraseImported

Keywords - Ligandi

CopperCombined sources, ManganeseCombined sources, Metal-bindingCombined sources, ZincCombined sources

Enzyme and pathway databases

BRENDAi5.3.1.14. 5158.

Names & Taxonomyi

Protein namesi
Submitted name:
L-rhamnose isomeraseImported
Gene namesi
Name:L-RhIImported
OrganismiPseudomonas stutzeri (Pseudomonas perfectomarina)Imported
Taxonomic identifieri316 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Interactioni

Protein-protein interaction databases

MINTiMINT-7384859.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HCVX-ray2.00A/B/C/D1-430[»]
2I56X-ray1.97A/B/C/D1-430[»]
2I57X-ray1.97A/B/C/D1-430[»]
3ITLX-ray1.70A/B/C/D1-430[»]
3ITOX-ray1.90A/B/C/D1-430[»]
3ITTX-ray1.96A/B/C/D1-430[»]
3ITVX-ray1.60A/B/C/D1-430[»]
3ITXX-ray1.80A/B/C/D1-430[»]
3ITYX-ray1.84A/B/C/D1-430[»]
3IUDX-ray2.44A/B/C/D1-430[»]
3IUHX-ray2.00A/B/C/D1-430[»]
3IUIX-ray2.30A/B/C/D1-430[»]
3M0HX-ray1.58A/B/C/D1-430[»]
3M0LX-ray1.85A/B/C/D1-430[»]
3M0MX-ray1.45A/B/C/D1-430[»]
3M0VX-ray1.79A/B/C/D1-430[»]
3M0XX-ray1.79A/B/C/D1-430[»]
3M0YX-ray1.96A/B/C/D1-430[»]
4GJIX-ray1.70A/B/C/D1-430[»]
4GJJX-ray2.38A/B/C/D1-430[»]
ProteinModelPortaliQ75WH8.
SMRiQ75WH8. Positions 3-430.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ75WH8.

Family & Domainsi

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
InterProiIPR013451. L_rhamnose_iso.
IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PfamiPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
SUPFAMiSSF51658. SSF51658. 1 hit.
TIGRFAMsiTIGR02629. L_rham_iso_rhiz. 1 hit.

Sequencei

Sequence statusi: Complete.

Q75WH8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEFRIAQDV VARENDRRAS ALKEDYEALG ANLARRGVDI EAVTAKVEKF
60 70 80 90 100
FVAVPSWGVG TGGTRFARFP GTGEPRGIFD KLDDCAVIQQ LTRATPNVSL
110 120 130 140 150
HIPWDKADPK ELKARGDALG LGFDAMNSNT FSDAPGQAHS YKYGSLSHTD
160 170 180 190 200
AATRAQAVEH NLECIEIGKA IGSKALTVWI GDGSNFPGQS NFTRAFERYL
210 220 230 240 250
SAMAEIYKGL PDDWKLFSEH KMYEPAFYST VVQDWGTNYL IAQTLGPKAQ
260 270 280 290 300
CLVDLGHHAP NTNIEMIVAR LIQFGKLGGF HFNDSKYGDD DLDAGAIEPY
310 320 330 340 350
RLFLVFNELV DAEARGVKGF HPAHMIDQSH NVTDPIESLI NSANEIRRAY
360 370 380 390 400
AQALLVDRAA LSGYQEDNDA LMATETLKRA YRTDVEPILA EARRRTGGAV
410 420 430
DPVATYRASG YRARVAAERP ASVAGGGGII
Length:430
Mass (Da):46,975
Last modified:July 5, 2004 - v1
Checksum:i2E2FBA87068472A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB121136 Genomic DNA. Translation: BAD14073.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB121136 Genomic DNA. Translation: BAD14073.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HCVX-ray2.00A/B/C/D1-430[»]
2I56X-ray1.97A/B/C/D1-430[»]
2I57X-ray1.97A/B/C/D1-430[»]
3ITLX-ray1.70A/B/C/D1-430[»]
3ITOX-ray1.90A/B/C/D1-430[»]
3ITTX-ray1.96A/B/C/D1-430[»]
3ITVX-ray1.60A/B/C/D1-430[»]
3ITXX-ray1.80A/B/C/D1-430[»]
3ITYX-ray1.84A/B/C/D1-430[»]
3IUDX-ray2.44A/B/C/D1-430[»]
3IUHX-ray2.00A/B/C/D1-430[»]
3IUIX-ray2.30A/B/C/D1-430[»]
3M0HX-ray1.58A/B/C/D1-430[»]
3M0LX-ray1.85A/B/C/D1-430[»]
3M0MX-ray1.45A/B/C/D1-430[»]
3M0VX-ray1.79A/B/C/D1-430[»]
3M0XX-ray1.79A/B/C/D1-430[»]
3M0YX-ray1.96A/B/C/D1-430[»]
4GJIX-ray1.70A/B/C/D1-430[»]
4GJJX-ray2.38A/B/C/D1-430[»]
ProteinModelPortaliQ75WH8.
SMRiQ75WH8. Positions 3-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-7384859.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi5.3.1.14. 5158.

Miscellaneous databases

EvolutionaryTraceiQ75WH8.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
InterProiIPR013451. L_rhamnose_iso.
IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PfamiPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
SUPFAMiSSF51658. SSF51658. 1 hit.
TIGRFAMsiTIGR02629. L_rham_iso_rhiz. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning, nucleotide sequence, and overexpression of the L-rhamnose isomerase gene from Pseudomonas stutzeri in Escherichia coli."
    Leang K., Takada G., Ishimura A., Okita M., Izumori K.
    Appl. Environ. Microbiol. 70:3298-3304(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "The structures of L-rhamnose isomerase from Pseudomonas stutzeri in complexes with L-rhamnose and D-allose provide insights into broad substrate specificity."
    Yoshida H., Yamada M., Ohyama Y., Takada G., Izumori K., Kamitori S.
    J. Mol. Biol. 365:1505-1516(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) IN COMPLEX WITH ZINC.
  3. "Catalytic reaction mechanism of Pseudomonas stutzeri L-rhamnose isomerase deduced from X-ray structures."
    Yoshida H., Yamaji M., Ishii T., Izumori K., Kamitori S.
    FEBS J. 277:1045-1057(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH COPPER; MANGANESE AND ZINC.
  4. "Elucidation of the role of Ser329 and the C-terminal region in the catalytic activity of Pseudomonas stutzeri L-rhamnose isomerase."
    Yoshida H., Takeda K., Izumori K., Kamitori S.
    Protein Eng. Des. Sel. 23:919-927(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH MANGANESE.
  5. "Structure of l-rhamnose isomerase in complex with l-rhamnopyranose demonstrates the sugar-ring opening mechanism and the role of a substrate sub-binding site."
    Yoshida H., Yoshihara A., Teraoka M., Yamashita S., Izumori K., Kamitori S.
    FEBS Open Bio 3:35-40(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH MANGANESE.

Entry informationi

Entry nameiQ75WH8_PSEST
AccessioniPrimary (citable) accession number: Q75WH8
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: April 1, 2015
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.