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Gellan lyase (EC 4.2.2.25) [Cleaved into: N-terminal gellan lyase; C-terminal gellan lyase]

 GELLY_BACSP             Reviewed;        2475 AA.
O82833;
16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 77.
RecName: Full=Gellan lyase;
EC=4.2.2.25;
Contains:
RecName: Full=N-terminal gellan lyase;
Contains:
RecName: Full=C-terminal gellan lyase;
Flags: Precursor;
Bacillus sp.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=1409;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-45,
FUNCTION, AND CATALYTIC ACTIVITY.
STRAIN=GL1;
PubMed=9633595; DOI=10.1006/abbi.1998.0674;
Hashimoto W., Sato N., Kimura S., Murata K.;
"Polysaccharide lyase: molecular cloning of gellan lyase gene and
formation of the lyase from a huge precursor protein in Bacillus sp.
GL1.";
Arch. Biochem. Biophys. 354:31-39(1998).
[2]
PROTEIN SEQUENCE OF 36-41; 1169-1194 AND 1203-1205, FUNCTION,
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PROTEOLYTIC
PROCESSING.
STRAIN=GL1;
PubMed=14759609; DOI=10.1016/j.abb.2003.12.015;
Miyake O., Kobayashi E., Nankai H., Hashimoto W., Mikami B.,
Murata K.;
"Posttranslational processing of polysaccharide lyase: maturation
route for gellan lyase in Bacillus sp. GL1.";
Arch. Biochem. Biophys. 422:211-220(2004).
[3]
CATALYTIC ACTIVITY.
STRAIN=GL1;
PubMed=9056228; DOI=10.1006/abbi.1996.9851;
Hashimoto W., Maesaka K., Sato N., Kimura S., Yamamoto K., Kumagai H.,
Murata K.;
"Microbial system for polysaccharide depolymerization: enzymatic route
for gellan depolymerization by Bacillus sp. GL1.";
Arch. Biochem. Biophys. 339:17-23(1997).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:14759609, ECO:0000269|PubMed:9633595}.
-!- CATALYTIC ACTIVITY: 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. {ECO:0000269|PubMed:14759609,
ECO:0000269|PubMed:9056228, ECO:0000269|PubMed:9633595}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.0 in potassium phosphate and 7.5 in HEPES
buffer. {ECO:0000269|PubMed:14759609};
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: 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. {ECO:0000269|PubMed:14759609}.
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EMBL; AB006853; BAA29068.1; -; Genomic_DNA.
PIR; T00047; T00047.
ProteinModelPortal; O82833; -.
SMR; O82833; -.
KEGG; ag:BAA29068; -.
KO; K20610; -.
BioCyc; MetaCyc:MONOMER-16405; -.
BRENDA; 4.2.2.25; 691.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR002102; Cohesin_dom.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR002509; NODB_dom.
Pfam; PF00963; Cohesin; 1.
Pfam; PF01522; Polysacc_deac_1; 1.
SMART; SM00060; FN3; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF88713; SSF88713; 1.
PROSITE; PS50853; FN3; 1.
PROSITE; PS51677; NODB; 1.
1: Evidence at protein level;
Direct protein sequencing; Lyase; Secreted; Signal.
SIGNAL 1 35 {ECO:0000269|PubMed:14759609,
ECO:0000269|PubMed:9633595}.
CHAIN 36 2475 Gellan lyase.
/FTId=PRO_0000424089.
CHAIN 36 1205 N-terminal gellan lyase.
/FTId=PRO_0000424090.
CHAIN 1206 2475 C-terminal gellan lyase.
/FTId=PRO_0000424091.
DOMAIN 623 708 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1295 1518 NodB homology. {ECO:0000255|PROSITE-
ProRule:PRU01014}.
DOMAIN 2111 2223 Cohesin.
COMPBIAS 2024 2107 Ala-rich.
SITE 1205 1206 Cleavage.
SEQUENCE 2475 AA; 263045 MW; 0184ED2F01CAFDF2 CRC64;
MRFSWKKLVS AALVMALLVG IVYPAASGRG AVASAASGTT VELVPTDDAF TSAVAKDANA
NGTWMQLKGS IGGQRYIYMK FDLTALAGVE ADRIENAKVW LKKMGTNGTA MTVGLRAVDD
TSWSESTLTW NNAPVYGSQV LSQQSVLSTP DVYYPFDLDE YLKTQLAAGK SKLAIAFVPI
STLNENMEFY ARESTANTPK LVVELKDEPP APTGLMQLVQ SFGGHNKGHL RVVEFDATPA
STTGNGTVGI TADGAAPAAA ADFPIALRFG TDGTIKAANA AGFESKTPVN YTAGQKYHVK
AMINLSLGTY DLWLTPPNAG QPVLLAADYA FAASAPALND IGGVHATADA QSTDVPAVAN
ARLIADHFVS KAPFKDEQGQ SLAIRLESDN SLANRSYAIK FDMNLTGNPL ETDALISYAD
RSVTLNGFPD LAYIVRSNFG NFDVRNDNVY ASSHPSTAQS NRTYQVEVRI NPASGTGQPT
RTYDVWIAPE GEQPVQLADQ FKARNYANTG YALNNIGQAF VYSQADGLLS IDNHVVQDGQ
RLDEALARVN AASGEAAMTA ALESNALGLP MERYRLMDAA KRAQVAQDVL AGRPAEGYAH
ALSVQAVFVS AVANRLDTEN PTAPANVQVA ISNTMQAHVS WTASSDDTGI LYYKVFRDGA
LVGTVTNATS FVDNGLAPAT EYTYVVKAYD LVLKEAVSQP ATATSPGEQA QVRIPFSAEA
IATAFGQPLL DYNLETHSGT LKWVMEWREE YEKSANALKL LTLLSASAPD YIGPDGVTTA
SAKALQHLRS VTAGGNEPGF AGNGLSGQGY MPLLSAIVMA KKKAPAIWNA LTAAEKEKLD
LMILAGLYGA KFAYDDENDN KTGIDATGNF DKEWNPNHRS GIAGAIMAMY YFEDAQWLND
QMRSFNYDDW LARLTAAGLT NVRTIYQNSG KTLTEREIRK DAAGDGFVYK GHPLSQPGKI
MAEFVNYTFS HPVSPVGGFD SGIGKYRGYI VDGQDDLPNL GADSMGFEFD TLDANGKRSS
LVYVFMGWKP NVDAITPVLL LDNIDSGLTS AETRDVVSRL SIGTTDMLYK NEHGYMTYAK
GVNEGVKSLN GPILTINEEI WNRILNNPAA PMEAVNQASS AGQMRTALEA SALGMILYGY
GALSETGKNA VAQHVLDARP AAGYANKAAA QNELYEGVRL QALLALSQAQ TAEQMRSALE
SRALGLYKPK YETASQDKKQ FVAQYLLDNK PADGFLTKTE VREQVESALE PQGNQLRNLP
PLASGEKRIN LADYDHWPQQ HGDAEVALWA DDKTGAFSLT IDDNFENEHD TWRSLAQQYG
FKFSWFVITS LIKDPNKWRT LAAEGHEIGS HTVTHEDKGS TLDPAHLHSE YADSQALLNT
IEGVRATTLA YPFGSGREDI AAEYYIAARG TVGLPNPADS INYMNTQSLS VRPGSLELTN
QAANGNSVEA MVKTLVDPNH KVWSASYYRG WSNMLVHSLN ESGKTPSDGV TRTSRDLTQY
LLTLLDTYRD QIWVGRYGDI VRYSQQRDTA HIVVTRKDDR KITFNLTDRM DDTLFDYPLT
VKVRVDDAWS DIGATQAGEP IPFVETIRDG KRYLLVKAVP DKGSVSIVPD AASPLNVVNG
AVTSEQMLSA IAAPGLGLDL GEFNALGAGK KRMVGSRLLE VRPADGYADA AALQDALDAA
VEEANNAPSL SENASLSDLK VNGVTIAGFA PETYAYDIML PEGTTALPVV SFKVADTGKA
TAVLQNAPAL PGTAKVTVTA EDNWTVATYT LRFQVRISAL QRVNTAPDAS AMRTAIENAA
LGLVLAAYNG LTSEQKNSVA ASVLTHRPAT GYADVQAVQA ELNAALPKIN APLLAHAIVD
QLNPDTVSTA NWTNLYGGTS GRKGGVYMKF NIASLAGLEA DAIGDAKVQF FTTREGTVIG
YAAPSSWEAP LTWNTQPLAD LKNSNMAALA EIGRTAVQAT GANYEMNITQ YVKDAAAADK
TELSLVLLGS NNTNITMQKI PTAFALSVTL ATYGEPNPEP SPLAAVNEAG DAAAMQGAIA
AVELDLNLTA YNGLTAAQRI DVAQALLDNR PAAGYAHALA VQVALDAAVA AAQPANQAPG
GTLAASAEQL QPGQQLELTV GVSDASRFTG ADILVHYDPQ ALTFATELYE GVRMLKAEAI
ASLQANYQVA AAMAEQPGTI KILLFTAGAG QPLSGTLPLF KLRASVKDDA QTGVSTAVSL
SDFELTFEGE DSVWPDTTRA AVSLQIAAHP VEADKTALIA KIAHAQALLT GATVGANPGQ
YPQAAYDALA DAIGLAEEKR DLTGVSQAAV DEAVASLGTA EQQFLNAVIP GVPADLTALN
AAIAKAQRLH DNGPYGEKIG QYPQSAKVPL KSALDAAKAV GGSGASSQES VNAAAASLNG
AIQTFERSLV TLVGGGATKV GIRDLSIVAK YYGVTSSDPN WGKVSAAAID GGNEITIEVL
AAVARMILAD WAAGQ


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