NIGP_LACP7
ID NIGP_LACP7 Reviewed; 753 AA.
AC A9KT32;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Nigerose phosphorylase;
DE EC=2.4.1.279 {ECO:0000269|PubMed:21808968};
GN OrderedLocusNames=Cphy_1874;
OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS (Clostridium phytofermentans).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=357809;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RX PubMed=21808968; DOI=10.1007/s00253-011-3515-9;
RA Nihira T., Nakai H., Chiku K., Kitaoka M.;
RT "Discovery of nigerose phosphorylase from Clostridium phytofermentans.";
RL Appl. Microbiol. Biotechnol. 93:1513-1522(2012).
CC -!- FUNCTION: Catalyzes the reversible phosphorolysis of nigerose. Also
CC shows a weak activity on kojibiose. {ECO:0000269|PubMed:21808968}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=nigerose + phosphate = beta-D-glucose 1-phosphate + D-glucose;
CC Xref=Rhea:RHEA:32523, ChEBI:CHEBI:4167, ChEBI:CHEBI:7570,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57684; EC=2.4.1.279;
CC Evidence={ECO:0000269|PubMed:21808968};
CC -!- ACTIVITY REGULATION: Does not require divalent metal ions.
CC {ECO:0000269|PubMed:21808968}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 mM for nigerose {ECO:0000269|PubMed:21808968};
CC KM=0.2 mM for phosphate {ECO:0000269|PubMed:21808968};
CC KM=3.3 mM for D-glucose {ECO:0000269|PubMed:21808968};
CC Note=kcat is 67 sec(-1) for nigerose. kcat is 110 sec(-1) for D-
CC glucose.;
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:21808968};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:21808968};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21808968}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:21808968}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR EMBL; CP000885; ABX42243.1; -; Genomic_DNA.
DR RefSeq; WP_012199897.1; NC_010001.1.
DR AlphaFoldDB; A9KT32; -.
DR SMR; A9KT32; -.
DR STRING; 357809.Cphy_1874; -.
DR CAZy; GH65; Glycoside Hydrolase Family 65.
DR EnsemblBacteria; ABX42243; ABX42243; Cphy_1874.
DR KEGG; cpy:Cphy_1874; -.
DR eggNOG; COG1554; Bacteria.
DR HOGENOM; CLU_006285_2_1_9; -.
DR OMA; ECAKFYY; -.
DR OrthoDB; 179460at2; -.
DR BRENDA; 2.4.1.279; 10424.
DR Proteomes; UP000000370; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IDA:CACAO.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005194; Glyco_hydro_65_C.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR Pfam; PF03633; Glyco_hydro_65C; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..753
FT /note="Nigerose phosphorylase"
FT /id="PRO_0000418723"
FT ACT_SITE 490
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 348..349
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 604..605
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
SQ SEQUENCE 753 AA; 87173 MW; D8AF1D004AF8FCC1 CRC64;
MNWTLTNSSL DKDSITSNGN RFLIGNGYLG IRGTLEEYRK EYFPAINLAG IYDQVGEGWR
EPLNAPNALY TRIEVDEVEY QLPKIEPRYH ELSLDYRHGI LDRQTVWASN KGTIIVKSSR
FASMKEKHLV VLNYSITADY DCEIIVYTGI DGSVWDIHGP HYDKVEFQKQ LLRHNETEIL
NEKYLLESES KWNGHRLSIA AQTHENKDIV YVTEDIICNK EAKIELIESD KECLRKLTFH
GKAKEEINFT KYITVFTSKD CVDYKEQSIK IVNHAKDTGY ERLQEEHKNV WEQLWNISEV
TIEGDDEAND ALNYSLYHLH CIAPRHSKSL SIAARGLSGQ TYKGAVFWDT EMFMLDFFLY
TQPEVAKTLL RYRIDTLEGA KKKAKLYGYE GAFYAWESQE GGYDACSDYN VTDVFTKRPM
RTYFKDKQVH ISSAIVYGIR SYLNYTNDFS ILAEGGAETI LECAKFYYSL LEKKIGKEYY
EIHDVIGPDE YHERVNNNAY TNRMAKLTFE TAIDILDHEK NKDEEFYIKL LKQYEIKDLL
DKLKDACNKL YIPKPKDNSD LIEQFDGFFE LEDVSLEEVR SRLLHEKEYW GGAYGVASHT
QVIKQADVVT MLVLFKEEYQ REVLQQNLNY YEPRTEHGSS LSACMYSLLY CMCDQPQYAY
PFFMKSALAD WNGKGKEWAG LVYIGGTHPA AAGGAYMTAI KGFGGFQIEN GVIKATPRLP
KHWVRLKYRV LYQGAIYEID ASKEQVSISK IEM
