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P12851

- XYLA_ACTM4

UniProt

P12851 - XYLA_ACTM4

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Protein

Xylose isomerase

Gene

xylA

Organism
Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-xylopyranose = D-xylulose.

Cofactori

Mg2+Note: Binds 2 magnesium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei54 – 541
Active sitei57 – 571By similarity
Metal bindingi181 – 1811Magnesium 1
Metal bindingi217 – 2171Magnesium 1
Metal bindingi217 – 2171Magnesium 2
Metal bindingi220 – 2201Magnesium 2
Metal bindingi245 – 2451Magnesium 1
Metal bindingi255 – 2551Magnesium 2
Metal bindingi257 – 2571Magnesium 2
Metal bindingi292 – 2921Magnesium 1

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. xylose isomerase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. D-xylose metabolic process Source: UniProtKB-HAMAP
  2. pentose-phosphate shunt Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Pentose shunt, Xylose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciAMIS512565:GL7J-1062-MONOMER.
SABIO-RKP12851.

Names & Taxonomyi

Protein namesi
Recommended name:
Xylose isomerase (EC:5.3.1.5)
Gene namesi
Name:xylA
Synonyms:XI
Ordered Locus Names:AMIS_10350
OrganismiActinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431)
Taxonomic identifieri512565 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeActinoplanes
ProteomesiUP000007882: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 394393Xylose isomerasePRO_0000195757Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 93Combined sources
Beta strandi11 – 144Combined sources
Helixi15 – 184Combined sources
Helixi36 – 4611Combined sources
Beta strandi49 – 524Combined sources
Helixi55 – 584Combined sources
Helixi65 – 8218Combined sources
Beta strandi88 – 903Combined sources
Beta strandi94 – 963Combined sources
Helixi97 – 993Combined sources
Helixi109 – 12921Combined sources
Beta strandi133 – 1375Combined sources
Beta strandi141 – 1455Combined sources
Helixi146 – 1483Combined sources
Helixi151 – 17222Combined sources
Beta strandi177 – 1815Combined sources
Beta strandi184 – 19310Combined sources
Helixi196 – 2038Combined sources
Beta strandi206 – 2083Combined sources
Helixi209 – 2113Combined sources
Beta strandi212 – 2143Combined sources
Helixi218 – 2225Combined sources
Turni223 – 2253Combined sources
Helixi228 – 23811Combined sources
Beta strandi244 – 2463Combined sources
Beta strandi251 – 2544Combined sources
Beta strandi262 – 2643Combined sources
Helixi265 – 27612Combined sources
Helixi279 – 2813Combined sources
Beta strandi289 – 2913Combined sources
Helixi301 – 32727Combined sources
Helixi329 – 3379Combined sources
Helixi341 – 3444Combined sources
Helixi354 – 3596Combined sources
Helixi361 – 3633Combined sources
Turni364 – 3663Combined sources
Helixi369 – 3735Combined sources
Helixi379 – 39012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BHWX-ray4.10A/B/C/D2-394[»]
1XIMX-ray2.20A/B/C/D2-394[»]
1XINX-ray2.40A/B/C/D2-394[»]
2XIMX-ray2.30A/B/C/D2-394[»]
2XINX-ray2.30A/B/C/D2-394[»]
3XIMX-ray2.30A/B/C/D2-394[»]
3XINX-ray2.30A/B/C/D2-394[»]
4XIMX-ray2.30A/B/C/D2-394[»]
5XIMX-ray2.60A/B/C/D2-394[»]
5XINX-ray2.30A/B/C/D2-394[»]
6XIMX-ray2.50A/B/C/D2-394[»]
7XIMX-ray2.40A/B/C/D2-394[»]
8XIMX-ray2.40A/B/C/D2-394[»]
9XIMX-ray2.40A/B/C/D2-394[»]
ProteinModelPortaliP12851.
SMRiP12851. Positions 3-394.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12851.

Family & Domainsi

Sequence similaritiesi

Belongs to the xylose isomerase family.Curated

Phylogenomic databases

KOiK01805.
OMAiDLIPIDA.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00455. Xylose_isom_A.
InterProiIPR013022. Xyl_isomerase-like_TIM-brl.
IPR013453. XylA_actinobac.
IPR001998. Xylose_isomerase.
[Graphical view]
PfamiPF01261. AP_endonuc_2. 1 hit.
[Graphical view]
PRINTSiPR00688. XYLOSISMRASE.
SUPFAMiSSF51658. SSF51658. 1 hit.
TIGRFAMsiTIGR02631. xylA_Arthro. 1 hit.
PROSITEiPS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12851-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVQATREDK FSFGLWTVGW QARDAFGDAT RTALDPVEAV HKLAEIGAYG
60 70 80 90 100
ITFHDDDLVP FGSDAQTRDG IIAGFKKALD ETGLIVPMVT TNLFTHPVFK
110 120 130 140 150
DGGFTSNDRS VRRYAIRKVL RQMDLGAELG AKTLVLWGGR EGAEYDSAKD
160 170 180 190 200
VSAALDRYRE ALNLLAQYSE DRGYGLRFAI EPKPNEPRGD ILLPTAGHAI
210 220 230 240 250
AFVQELERPE LFGINPETGH EQMSNLNFTQ GIAQALWHKK LFHIDLNGQH
260 270 280 290 300
GPKFDQDLVF GHGDLLNAFS LVDLLENGPD GAPAYDGPRH FDYKPSRTED
310 320 330 340 350
YDGVWESAKA NIRMYLLLKE RAKAFRADPE VQEALAASKV AELKTPTLNP
360 370 380 390
GEGYAELLAD RSAFEDYDAD AVGAKGFGFV KLNQLAIEHL LGAR
Length:394
Mass (Da):43,499
Last modified:January 23, 2007 - v3
Checksum:i764B1FC35AE7A780
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16042 Genomic DNA. Translation: CAA34164.1.
AP012319 Genomic DNA. Translation: BAL86255.1.
PIRiS05998. ISMAXM.
RefSeqiWP_014441152.1. NC_017093.1.
YP_005460771.1. NC_017093.1.

Genome annotation databases

EnsemblBacteriaiBAL86255; BAL86255; AMIS_10350.
GeneIDi12051265.
KEGGiams:AMIS_10350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16042 Genomic DNA. Translation: CAA34164.1 .
AP012319 Genomic DNA. Translation: BAL86255.1 .
PIRi S05998. ISMAXM.
RefSeqi WP_014441152.1. NC_017093.1.
YP_005460771.1. NC_017093.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BHW X-ray 4.10 A/B/C/D 2-394 [» ]
1XIM X-ray 2.20 A/B/C/D 2-394 [» ]
1XIN X-ray 2.40 A/B/C/D 2-394 [» ]
2XIM X-ray 2.30 A/B/C/D 2-394 [» ]
2XIN X-ray 2.30 A/B/C/D 2-394 [» ]
3XIM X-ray 2.30 A/B/C/D 2-394 [» ]
3XIN X-ray 2.30 A/B/C/D 2-394 [» ]
4XIM X-ray 2.30 A/B/C/D 2-394 [» ]
5XIM X-ray 2.60 A/B/C/D 2-394 [» ]
5XIN X-ray 2.30 A/B/C/D 2-394 [» ]
6XIM X-ray 2.50 A/B/C/D 2-394 [» ]
7XIM X-ray 2.40 A/B/C/D 2-394 [» ]
8XIM X-ray 2.40 A/B/C/D 2-394 [» ]
9XIM X-ray 2.40 A/B/C/D 2-394 [» ]
ProteinModelPortali P12851.
SMRi P12851. Positions 3-394.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAL86255 ; BAL86255 ; AMIS_10350 .
GeneIDi 12051265.
KEGGi ams:AMIS_10350.

Phylogenomic databases

KOi K01805.
OMAi DLIPIDA.

Enzyme and pathway databases

BioCyci AMIS512565:GL7J-1062-MONOMER.
SABIO-RK P12851.

Miscellaneous databases

EvolutionaryTracei P12851.

Family and domain databases

Gene3Di 3.20.20.150. 1 hit.
HAMAPi MF_00455. Xylose_isom_A.
InterProi IPR013022. Xyl_isomerase-like_TIM-brl.
IPR013453. XylA_actinobac.
IPR001998. Xylose_isomerase.
[Graphical view ]
Pfami PF01261. AP_endonuc_2. 1 hit.
[Graphical view ]
PRINTSi PR00688. XYLOSISMRASE.
SUPFAMi SSF51658. SSF51658. 1 hit.
TIGRFAMsi TIGR02631. xylA_Arthro. 1 hit.
PROSITEi PS51415. XYLOSE_ISOMERASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Xylose isomerase from Actinoplanes missouriensis: primary structure of the gene and the protein."
    Amore R., Hollenberg C.P.
    Nucleic Acids Res. 17:7515-7515(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431.
  2. "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC 102363)."
    Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H., Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.
    Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NCIMB 12654 / NBRC 102363 / 431.
  3. "Structural analysis of the 2.8 A model of Xylose isomerase from Actinoplanes missouriensis."
    Rey F., Jenkins J., Janin J., Lasters I., Alard P., Claessens M., Matthyssens G., Wodak S.J.
    Proteins 4:165-172(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  4. "Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 1. Crystallography and site-directed mutagenesis of metal binding sites."
    Jenkins J., Janin J., Rey F., Chiadmi M., van Tilbeurgh H., Lasters I., de Maeyer M., van Belle D., Wodak S.J., Lauwereys M., Stanssens P., Mrabet N.T., Snauwaert J., Matthyssens G., Lambeir A.-M.
    Biochemistry 31:5449-5458(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  5. "Multiwavelength anomalous solvent contrast (MASC): derivation of envelope structure-factor amplitudes and comparison with model values."
    Ramin M., Shepard W., Fourme R., Kahn R.
    Acta Crystallogr. D 55:157-167(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS).
  6. "Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 2. Site-directed mutagenesis of the xylose binding site."
    Lambeir A.-M., Lauwereys M., Stanssens P., Mrabet N.T., Snauwaert J., van Tilbeurgh H., Matthyssens G., Lasters I., de Maeyer M., Wodak S.J., Jenkins J., Chiadmi M., Janin J.
    Biochemistry 31:5459-5466(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  7. "Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 3. Changing metal specificity and the pH profile by site-directed mutagenesis."
    van Tilbeurgh H., Jenkins J., Chiadmi M., Janin J., Wodak S.J., Mrabet N.T., Lambeir A.-M.
    Biochemistry 31:5467-5472(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.

Entry informationi

Entry nameiXYLA_ACTM4
AccessioniPrimary (citable) accession number: P12851
Secondary accession number(s): I0GZR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3