Skip Header

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

O82833

- GELLY_BACSP

UniProt

O82833 - GELLY_BACSP

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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-KW
Complete GO annotation...

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

        10         20         30         40         50
MRFSWKKLVS AALVMALLVG IVYPAASGRG AVASAASGTT VELVPTDDAF
60 70 80 90 100
TSAVAKDANA NGTWMQLKGS IGGQRYIYMK FDLTALAGVE ADRIENAKVW
110 120 130 140 150
LKKMGTNGTA MTVGLRAVDD TSWSESTLTW NNAPVYGSQV LSQQSVLSTP
160 170 180 190 200
DVYYPFDLDE YLKTQLAAGK SKLAIAFVPI STLNENMEFY ARESTANTPK
210 220 230 240 250
LVVELKDEPP APTGLMQLVQ SFGGHNKGHL RVVEFDATPA STTGNGTVGI
260 270 280 290 300
TADGAAPAAA ADFPIALRFG TDGTIKAANA AGFESKTPVN YTAGQKYHVK
310 320 330 340 350
AMINLSLGTY DLWLTPPNAG QPVLLAADYA FAASAPALND IGGVHATADA
360 370 380 390 400
QSTDVPAVAN ARLIADHFVS KAPFKDEQGQ SLAIRLESDN SLANRSYAIK
410 420 430 440 450
FDMNLTGNPL ETDALISYAD RSVTLNGFPD LAYIVRSNFG NFDVRNDNVY
460 470 480 490 500
ASSHPSTAQS NRTYQVEVRI NPASGTGQPT RTYDVWIAPE GEQPVQLADQ
510 520 530 540 550
FKARNYANTG YALNNIGQAF VYSQADGLLS IDNHVVQDGQ RLDEALARVN
560 570 580 590 600
AASGEAAMTA ALESNALGLP MERYRLMDAA KRAQVAQDVL AGRPAEGYAH
610 620 630 640 650
ALSVQAVFVS AVANRLDTEN PTAPANVQVA ISNTMQAHVS WTASSDDTGI
660 670 680 690 700
LYYKVFRDGA LVGTVTNATS FVDNGLAPAT EYTYVVKAYD LVLKEAVSQP
710 720 730 740 750
ATATSPGEQA QVRIPFSAEA IATAFGQPLL DYNLETHSGT LKWVMEWREE
760 770 780 790 800
YEKSANALKL LTLLSASAPD YIGPDGVTTA SAKALQHLRS VTAGGNEPGF
810 820 830 840 850
AGNGLSGQGY MPLLSAIVMA KKKAPAIWNA LTAAEKEKLD LMILAGLYGA
860 870 880 890 900
KFAYDDENDN KTGIDATGNF DKEWNPNHRS GIAGAIMAMY YFEDAQWLND
910 920 930 940 950
QMRSFNYDDW LARLTAAGLT NVRTIYQNSG KTLTEREIRK DAAGDGFVYK
960 970 980 990 1000
GHPLSQPGKI MAEFVNYTFS HPVSPVGGFD SGIGKYRGYI VDGQDDLPNL
1010 1020 1030 1040 1050
GADSMGFEFD TLDANGKRSS LVYVFMGWKP NVDAITPVLL LDNIDSGLTS
1060 1070 1080 1090 1100
AETRDVVSRL SIGTTDMLYK NEHGYMTYAK GVNEGVKSLN GPILTINEEI
1110 1120 1130 1140 1150
WNRILNNPAA PMEAVNQASS AGQMRTALEA SALGMILYGY GALSETGKNA
1160 1170 1180 1190 1200
VAQHVLDARP AAGYANKAAA QNELYEGVRL QALLALSQAQ TAEQMRSALE
1210 1220 1230 1240 1250
SRALGLYKPK YETASQDKKQ FVAQYLLDNK PADGFLTKTE VREQVESALE
1260 1270 1280 1290 1300
PQGNQLRNLP PLASGEKRIN LADYDHWPQQ HGDAEVALWA DDKTGAFSLT
1310 1320 1330 1340 1350
IDDNFENEHD TWRSLAQQYG FKFSWFVITS LIKDPNKWRT LAAEGHEIGS
1360 1370 1380 1390 1400
HTVTHEDKGS TLDPAHLHSE YADSQALLNT IEGVRATTLA YPFGSGREDI
1410 1420 1430 1440 1450
AAEYYIAARG TVGLPNPADS INYMNTQSLS VRPGSLELTN QAANGNSVEA
1460 1470 1480 1490 1500
MVKTLVDPNH KVWSASYYRG WSNMLVHSLN ESGKTPSDGV TRTSRDLTQY
1510 1520 1530 1540 1550
LLTLLDTYRD QIWVGRYGDI VRYSQQRDTA HIVVTRKDDR KITFNLTDRM
1560 1570 1580 1590 1600
DDTLFDYPLT VKVRVDDAWS DIGATQAGEP IPFVETIRDG KRYLLVKAVP
1610 1620 1630 1640 1650
DKGSVSIVPD AASPLNVVNG AVTSEQMLSA IAAPGLGLDL GEFNALGAGK
1660 1670 1680 1690 1700
KRMVGSRLLE VRPADGYADA AALQDALDAA VEEANNAPSL SENASLSDLK
1710 1720 1730 1740 1750
VNGVTIAGFA PETYAYDIML PEGTTALPVV SFKVADTGKA TAVLQNAPAL
1760 1770 1780 1790 1800
PGTAKVTVTA EDNWTVATYT LRFQVRISAL QRVNTAPDAS AMRTAIENAA
1810 1820 1830 1840 1850
LGLVLAAYNG LTSEQKNSVA ASVLTHRPAT GYADVQAVQA ELNAALPKIN
1860 1870 1880 1890 1900
APLLAHAIVD QLNPDTVSTA NWTNLYGGTS GRKGGVYMKF NIASLAGLEA
1910 1920 1930 1940 1950
DAIGDAKVQF FTTREGTVIG YAAPSSWEAP LTWNTQPLAD LKNSNMAALA
1960 1970 1980 1990 2000
EIGRTAVQAT GANYEMNITQ YVKDAAAADK TELSLVLLGS NNTNITMQKI
2010 2020 2030 2040 2050
PTAFALSVTL ATYGEPNPEP SPLAAVNEAG DAAAMQGAIA AVELDLNLTA
2060 2070 2080 2090 2100
YNGLTAAQRI DVAQALLDNR PAAGYAHALA VQVALDAAVA AAQPANQAPG
2110 2120 2130 2140 2150
GTLAASAEQL QPGQQLELTV GVSDASRFTG ADILVHYDPQ ALTFATELYE
2160 2170 2180 2190 2200
GVRMLKAEAI ASLQANYQVA AAMAEQPGTI KILLFTAGAG QPLSGTLPLF
2210 2220 2230 2240 2250
KLRASVKDDA QTGVSTAVSL SDFELTFEGE DSVWPDTTRA AVSLQIAAHP
2260 2270 2280 2290 2300
VEADKTALIA KIAHAQALLT GATVGANPGQ YPQAAYDALA DAIGLAEEKR
2310 2320 2330 2340 2350
DLTGVSQAAV DEAVASLGTA EQQFLNAVIP GVPADLTALN AAIAKAQRLH
2360 2370 2380 2390 2400
DNGPYGEKIG QYPQSAKVPL KSALDAAKAV GGSGASSQES VNAAAASLNG
2410 2420 2430 2440 2450
AIQTFERSLV TLVGGGATKV GIRDLSIVAK YYGVTSSDPN WGKVSAAAID
2460 2470
GGNEITIEVL AAVARMILAD WAAGQ
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 29, 2014
This is version 67 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