12OLP_LISIN
ID 12OLP_LISIN Reviewed; 1086 AA.
AC Q92AT0;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=1,2-beta-oligoglucan phosphorylase {ECO:0000305};
DE EC=2.4.1.333 {ECO:0000269|PubMed:24647662};
GN OrderedLocusNames=lin1839 {ECO:0000312|EMBL:CAC97070.1};
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262 {ECO:0000312|Proteomes:UP000002513};
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24647662; DOI=10.1371/journal.pone.0092353;
RA Nakajima M., Toyoizumi H., Abe K., Nakai H., Taguchi H., Kitaoka M.;
RT "1,2-beta-Oligoglucan phosphorylase from Listeria innocua.";
RL PLoS ONE 9:E92353-E92353(2014).
CC -!- FUNCTION: Catalyzes the reversible phosphorolysis of beta-(1->2)-D-
CC glucans. The minimum length of the substrate for the phosphorolytic
CC reaction is 3 D-glucose units. {ECO:0000269|PubMed:24647662}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->2)-beta-D-glucosyl](n) + phosphate = [(1->2)-beta-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:47684,
CC Rhea:RHEA-COMP:11881, Rhea:RHEA-COMP:11882, ChEBI:CHEBI:27517,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.333;
CC Evidence={ECO:0000269|PubMed:24647662};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.5 mM for (beta-(1->2)-D-glucans) x 2 units in the synthetic
CC reaction {ECO:0000269|PubMed:24647662};
CC KM=6.0 mM for (beta-(1->2)-D-glucans) x 3 units in the synthetic
CC reaction {ECO:0000269|PubMed:24647662};
CC KM=6.8 mM for (beta-(1->2)-D-glucans) x 4 units in the synthetic
CC reaction {ECO:0000269|PubMed:24647662};
CC KM=1.2 mM for alpha-D-glucose 1-phosphate in the synthetic reaction
CC {ECO:0000269|PubMed:24647662};
CC KM=1.0 mM for (beta-(1->2)-D-glucans) x 3 units in the phosphorolytic
CC reaction {ECO:0000269|PubMed:24647662};
CC KM=1.2 mM for (beta-(1->2)-D-glucans) x 4 units in the phosphorolytic
CC reaction {ECO:0000269|PubMed:24647662};
CC KM=1.8 mM for (beta-(1->2)-D-glucans) x 5 units in the phosphorolytic
CC reaction {ECO:0000269|PubMed:24647662};
CC Note=kcat is 97 sec(-1) for (beta-(1->2)-D-glucans) x 2 units in the
CC synthetic reaction. kcat is 110 sec(-1) for (beta-(1->2)-D-glucans) x
CC 3 units in the synthetic reaction. kcat is 90 sec(-1) for (beta-
CC (1->2)-D-glucans) x 4 units in the synthetic reaction. kcat is 43
CC sec(-1) for alpha-D-glucose 1-phosphate in the synthetic reaction.
CC kcat is 19 sec(-1) for (beta-(1->2)-D-glucans) x 3 units in the
CC phosphorolytic reaction. kcat is 30 sec(-1) for (beta-(1->2)-D-
CC glucans) x 4 units in the phosphorolytic reaction. kcat is 31 sec(-1)
CC for (beta-(1->2)-D-glucans) x 5 units in the phosphorolytic reaction.
CC {ECO:0000269|PubMed:24647662};
CC pH dependence:
CC Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:24647662};
CC Temperature dependence:
CC Optimum temperature is 37-45 degrees Celsius.
CC {ECO:0000269|PubMed:24647662};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:24647662}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 94 family. {ECO:0000305}.
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DR EMBL; AL596170; CAC97070.1; -; Genomic_DNA.
DR PIR; AF1662; AF1662.
DR RefSeq; WP_010990982.1; NC_003212.1.
DR AlphaFoldDB; Q92AT0; -.
DR SMR; Q92AT0; -.
DR STRING; 272626.lin1839; -.
DR CAZy; GH94; Glycoside Hydrolase Family 94.
DR EnsemblBacteria; CAC97070; CAC97070; CAC97070.
DR KEGG; lin:lin1839; -.
DR eggNOG; COG3459; Bacteria.
DR HOGENOM; CLU_009079_0_0_9; -.
DR OMA; VPHGLEQ; -.
DR OrthoDB; 279804at2; -.
DR BRENDA; 2.4.1.333; 3044.
DR Proteomes; UP000002513; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR033432; GH36_catalytic.
DR Pfam; PF17167; Glyco_hydro_36; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW Transferase.
FT CHAIN 1..1086
FT /note="1,2-beta-oligoglucan phosphorylase"
FT /id="PRO_0000432711"
FT ACT_SITE 738
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1086 AA; 122895 MW; 5D87750286582095 CRC64;
MTMLKEIKKA DLSAAFYPSG ELAWLKLKDI MLNQVIQNPL ENRLSQIYVR AHVGDKIEIY
PLLSRDAEVG FNENGVEYRG VVGPFRYSVQ MHFHTRGWFY DVTVDGDLEF DLVYLQDLGL
AEQAAVRTNE AYMSQYIDYH VTEGATGFTV QARQNQPQNE RFPAVQIGAL TKIVGYATDG
FDIYGTNYKL TSELANLKEK SLPSRVYQYE FAQISLQTEL FTNHGETIFY GYATENQPKA
SGAPFENLAE LKSNISEQPY QPSTKAILNK HIGTPITGET ISDSWLQENF PDRIQEEQQN
GALLSFFTPN YAHVVMREKE AELERPHGSI LLDKVDVLNP EATLSATTYM YGAFLSQLVA
GNTNMNKWNS HARNPLNILQ TSGLRIYIEL DSELRLLGVP SVWETSTNYS TWYYQWNGDL
ITVQTTLTAD SKEAFVTVHS EKGHSYKLVL TNQVTMGTNE YDTTVKKEIK DGIVTYFPAE
DSPILETYPA LQFRVDGTYN ELTDERYFAK DYVGTAGLDV FVFEPSDKAT FHVQAKLSDE
FSKPTEDLEA NNKVIRASYD ELTAQFHLNH QSTTAEKLNL TVYWYAHQML VHYASPHGLE
QYSGAAWGTR DVSQGPFEFF LATGNKAVLR KLVLTIFSHQ YQDTGDWPQW FMFDKYTSIQ
QEESHGDVIV WPLKIIGDYL EMSGDAGILE EAIPFVDRES KTFTKEQGTL LEHIELAVKT
IEARFMKGTA LSNYGDGDWD DTLQPANAQL KKNMVSSWTV ALTYQTFKRL AAFLPVGEKY
ETLAKNVQAD FAKYMTNDTD VIPGFLYLEE GKAPVWMIHP EDKETNIKYR LIPLTRSVIS
ELVDKKQASR NFEIIGEHLL HPDGVRLMSE PAHYAGGVST HFKRAEQAAN FGREVGLQYV
HAHIRYIEAL AKIGDKSAWH MLDVINPINI KEVVPNAALR QSNTYFSSSD AAFLDRYQAQ
NEFGRVKEGS IPVKGGWRIY SSGPGIYLHQ LISSVLGIRQ TEDALIFDPI LPEELDGLEC
HIELDNYPLD LTFESADEGS IVVNGEKQPV ENGANLYRTG ALILPKKNLT TKCSQITIKF
QKNNRL
