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O82833

- GELLY_BACSP

UniProt

O82833 - GELLY_BACSP

Protein

Gellan lyase

Gene
N/A
Organism
Bacillus sp.
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    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

    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

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 35352 PublicationsAdd
    BLAST
    Chaini36 – 24752440Gellan lyasePRO_0000424089Add
    BLAST
    Chaini36 – 12051170N-terminal gellan lyasePRO_0000424090Add
    BLAST
    Chaini1206 – 24751270C-terminal gellan lyasePRO_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.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliO82833.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini623 – 70886Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST
    Domaini1295 – 1518224NodB homologyPROSITE-ProRule annotationAdd
    BLAST
    Domaini2111 – 2223113CohesinAdd
    BLAST

    Compositional bias

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

    Sequence similaritiesi

    Contains 1 cohesin domain.Curated
    Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation
    Contains 1 NodB homology domain.PROSITE-ProRule annotation

    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: October 1, 2014
    This is version 66 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