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O82833

- GELLY_BACSP

UniProt

O82833 - GELLY_BACSP

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Protein
Gellan lyase
Gene
N/A
Organism
Bacillus sp.
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Cleaves the glycosidic bonds of gellan backbone and releases tetrasaccharide units of glucuronyl-glucosyl-rhamnosyl-glucose with unsaturated glucuronic acid at the non-reducing terminal. The enzyme is highly specific to the heteropolysaccharide gellan, especially deacetylated gellan.2 Publications

Catalytic activityi

Eliminative cleavage of beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyluronate bonds of gellan backbone releasing tetrasaccharides containing a 4-deoxy-4,5-unsaturated D-glucopyranosyluronic acid at the non-reducing end. The tetrasaccharide produced from deacetylated gellan is beta-D-4-deoxy-Delta(4)-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp.3 Publications

pH dependencei

Optimum pH is 6.0 in potassium phosphate and 7.5 in HEPES buffer.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1205 – 12062Cleavage

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Source: InterPro
  3. lyase activity Source: UniProtKB-KW

GO - Biological processi

  1. polysaccharide catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16405.

Names & Taxonomyi

Protein namesi
Recommended name:
Gellan lyase (EC:4.2.2.25)
Cleaved into the following 2 chains:
OrganismiBacillus sp.
Taxonomic identifieri1409 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 35352 Publications
Add
BLAST
Chaini36 – 24752440Gellan lyase
PRO_0000424089Add
BLAST
Chaini36 – 12051170N-terminal gellan lyase
PRO_0000424090Add
BLAST
Chaini1206 – 24751270C-terminal gellan lyase
PRO_0000424091Add
BLAST

Post-translational modificationi

Subject to proteolytic processing after secretion. Cleavage occurs between Gly-1205 and Leu-1206. This gives rise to a N-terminal gellan lyase of 130 kDa being the mature form of the gellan lyase. The function of C-terminal gellan lyase is not known.

Structurei

3D structure databases

ProteinModelPortaliO82833.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini623 – 70886Fibronectin type-III
Add
BLAST
Domaini1295 – 1518224NodB homology
Add
BLAST
Domaini2111 – 2223113Cohesin
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2024 – 210784Ala-rich
Add
BLAST

Sequence similaritiesi

Contains 1 cohesin domain.

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.20.20.370. 1 hit.
InterProiIPR002102. Cohesin_dom.
IPR003961. Fibronectin_type3.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR013783. Ig-like_fold.
IPR002509. Polysac_deacetylase.
[Graphical view]
PfamiPF00963. Cohesin. 1 hit.
PF00041. fn3. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
SMARTiSM00060. FN3. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 1 hit.
SSF88713. SSF88713. 1 hit.
PROSITEiPS50853. FN3. 1 hit.
PS51677. NODB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O82833-1 [UniParc]FASTAAdd to Basket

« Hide

MRFSWKKLVS AALVMALLVG IVYPAASGRG AVASAASGTT VELVPTDDAF     50
TSAVAKDANA NGTWMQLKGS IGGQRYIYMK FDLTALAGVE ADRIENAKVW 100
LKKMGTNGTA MTVGLRAVDD TSWSESTLTW NNAPVYGSQV LSQQSVLSTP 150
DVYYPFDLDE YLKTQLAAGK SKLAIAFVPI STLNENMEFY ARESTANTPK 200
LVVELKDEPP APTGLMQLVQ SFGGHNKGHL RVVEFDATPA STTGNGTVGI 250
TADGAAPAAA ADFPIALRFG TDGTIKAANA AGFESKTPVN YTAGQKYHVK 300
AMINLSLGTY DLWLTPPNAG QPVLLAADYA FAASAPALND IGGVHATADA 350
QSTDVPAVAN ARLIADHFVS KAPFKDEQGQ SLAIRLESDN SLANRSYAIK 400
FDMNLTGNPL ETDALISYAD RSVTLNGFPD LAYIVRSNFG NFDVRNDNVY 450
ASSHPSTAQS NRTYQVEVRI NPASGTGQPT RTYDVWIAPE GEQPVQLADQ 500
FKARNYANTG YALNNIGQAF VYSQADGLLS IDNHVVQDGQ RLDEALARVN 550
AASGEAAMTA ALESNALGLP MERYRLMDAA KRAQVAQDVL AGRPAEGYAH 600
ALSVQAVFVS AVANRLDTEN PTAPANVQVA ISNTMQAHVS WTASSDDTGI 650
LYYKVFRDGA LVGTVTNATS FVDNGLAPAT EYTYVVKAYD LVLKEAVSQP 700
ATATSPGEQA QVRIPFSAEA IATAFGQPLL DYNLETHSGT LKWVMEWREE 750
YEKSANALKL LTLLSASAPD YIGPDGVTTA SAKALQHLRS VTAGGNEPGF 800
AGNGLSGQGY MPLLSAIVMA KKKAPAIWNA LTAAEKEKLD LMILAGLYGA 850
KFAYDDENDN KTGIDATGNF DKEWNPNHRS GIAGAIMAMY YFEDAQWLND 900
QMRSFNYDDW LARLTAAGLT NVRTIYQNSG KTLTEREIRK DAAGDGFVYK 950
GHPLSQPGKI MAEFVNYTFS HPVSPVGGFD SGIGKYRGYI VDGQDDLPNL 1000
GADSMGFEFD TLDANGKRSS LVYVFMGWKP NVDAITPVLL LDNIDSGLTS 1050
AETRDVVSRL SIGTTDMLYK NEHGYMTYAK GVNEGVKSLN GPILTINEEI 1100
WNRILNNPAA PMEAVNQASS AGQMRTALEA SALGMILYGY GALSETGKNA 1150
VAQHVLDARP AAGYANKAAA QNELYEGVRL QALLALSQAQ TAEQMRSALE 1200
SRALGLYKPK YETASQDKKQ FVAQYLLDNK PADGFLTKTE VREQVESALE 1250
PQGNQLRNLP PLASGEKRIN LADYDHWPQQ HGDAEVALWA DDKTGAFSLT 1300
IDDNFENEHD TWRSLAQQYG FKFSWFVITS LIKDPNKWRT LAAEGHEIGS 1350
HTVTHEDKGS TLDPAHLHSE YADSQALLNT IEGVRATTLA YPFGSGREDI 1400
AAEYYIAARG TVGLPNPADS INYMNTQSLS VRPGSLELTN QAANGNSVEA 1450
MVKTLVDPNH KVWSASYYRG WSNMLVHSLN ESGKTPSDGV TRTSRDLTQY 1500
LLTLLDTYRD QIWVGRYGDI VRYSQQRDTA HIVVTRKDDR KITFNLTDRM 1550
DDTLFDYPLT VKVRVDDAWS DIGATQAGEP IPFVETIRDG KRYLLVKAVP 1600
DKGSVSIVPD AASPLNVVNG AVTSEQMLSA IAAPGLGLDL GEFNALGAGK 1650
KRMVGSRLLE VRPADGYADA AALQDALDAA VEEANNAPSL SENASLSDLK 1700
VNGVTIAGFA PETYAYDIML PEGTTALPVV SFKVADTGKA TAVLQNAPAL 1750
PGTAKVTVTA EDNWTVATYT LRFQVRISAL QRVNTAPDAS AMRTAIENAA 1800
LGLVLAAYNG LTSEQKNSVA ASVLTHRPAT GYADVQAVQA ELNAALPKIN 1850
APLLAHAIVD QLNPDTVSTA NWTNLYGGTS GRKGGVYMKF NIASLAGLEA 1900
DAIGDAKVQF FTTREGTVIG YAAPSSWEAP LTWNTQPLAD LKNSNMAALA 1950
EIGRTAVQAT GANYEMNITQ YVKDAAAADK TELSLVLLGS NNTNITMQKI 2000
PTAFALSVTL ATYGEPNPEP SPLAAVNEAG DAAAMQGAIA AVELDLNLTA 2050
YNGLTAAQRI DVAQALLDNR PAAGYAHALA VQVALDAAVA AAQPANQAPG 2100
GTLAASAEQL QPGQQLELTV GVSDASRFTG ADILVHYDPQ ALTFATELYE 2150
GVRMLKAEAI ASLQANYQVA AAMAEQPGTI KILLFTAGAG QPLSGTLPLF 2200
KLRASVKDDA QTGVSTAVSL SDFELTFEGE DSVWPDTTRA AVSLQIAAHP 2250
VEADKTALIA KIAHAQALLT GATVGANPGQ YPQAAYDALA DAIGLAEEKR 2300
DLTGVSQAAV DEAVASLGTA EQQFLNAVIP GVPADLTALN AAIAKAQRLH 2350
DNGPYGEKIG QYPQSAKVPL KSALDAAKAV GGSGASSQES VNAAAASLNG 2400
AIQTFERSLV TLVGGGATKV GIRDLSIVAK YYGVTSSDPN WGKVSAAAID 2450
GGNEITIEVL AAVARMILAD WAAGQ 2475
Length:2,475
Mass (Da):263,045
Last modified:November 1, 1998 - v1
Checksum:i0184ED2F01CAFDF2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB006853 Genomic DNA. Translation: BAA29068.1.
PIRiT00047.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB006853 Genomic DNA. Translation: BAA29068.1 .
PIRi T00047.

3D structure databases

ProteinModelPortali O82833.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16405.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
3.20.20.370. 1 hit.
InterProi IPR002102. Cohesin_dom.
IPR003961. Fibronectin_type3.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR013783. Ig-like_fold.
IPR002509. Polysac_deacetylase.
[Graphical view ]
Pfami PF00963. Cohesin. 1 hit.
PF00041. fn3. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view ]
SMARTi SM00060. FN3. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 1 hit.
SSF88713. SSF88713. 1 hit.
PROSITEi PS50853. FN3. 1 hit.
PS51677. NODB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Polysaccharide lyase: molecular cloning of gellan lyase gene and formation of the lyase from a huge precursor protein in Bacillus sp. GL1."
    Hashimoto W., Sato N., Kimura S., Murata K.
    Arch. Biochem. Biophys. 354:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-45, FUNCTION, CATALYTIC ACTIVITY.
    Strain: GL1.
  2. "Posttranslational processing of polysaccharide lyase: maturation route for gellan lyase in Bacillus sp. GL1."
    Miyake O., Kobayashi E., Nankai H., Hashimoto W., Mikami B., Murata K.
    Arch. Biochem. Biophys. 422:211-220(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 36-41; 1169-1194 AND 1203-1205, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PROTEOLYTIC PROCESSING.
    Strain: GL1.
  3. "Microbial system for polysaccharide depolymerization: enzymatic route for gellan depolymerization by Bacillus sp. GL1."
    Hashimoto W., Maesaka K., Sato N., Kimura S., Yamamoto K., Kumagai H., Murata K.
    Arch. Biochem. Biophys. 339:17-23(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
    Strain: GL1.

Entry informationi

Entry nameiGELLY_BACSP
AccessioniPrimary (citable) accession number: O82833
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: November 1, 1998
Last modified: December 11, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3