ID   PHSM_STRPN              Reviewed;         752 AA.
AC   P29849;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Maltodextrin phosphorylase;
DE            EC=2.4.1.1;
GN   Name=malP; OrderedLocusNames=SP_2106;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.
RX   PubMed=6297760; DOI=10.1016/0092-8674(82)90126-x;
RA   Lacks S.A., Dunn J.J., Greenberg B.;
RT   "Identification of base mismatches recognized by the heteroduplex-DNA-
RT   repair system of Streptococcus pneumoniae.";
RL   Cell 31:327-336(1982).
CC   -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC       carbohydrate metabolism. Enzymes from different sources differ in their
CC       regulatory mechanisms and in their natural substrates. However, all
CC       known phosphorylases share catalytic and structural properties.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC         glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC         Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000305}.
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DR   EMBL; AE005672; AAK76165.1; -; Genomic_DNA.
DR   EMBL; J01796; AAA26924.1; -; Genomic_DNA.
DR   PIR; D95246; D95246.
DR   RefSeq; WP_000950154.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; P29849; -.
DR   SMR; P29849; -.
DR   STRING; 170187.SP_2106; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   EnsemblBacteria; AAK76165; AAK76165; SP_2106.
DR   KEGG; spn:SP_2106; -.
DR   eggNOG; COG0058; Bacteria.
DR   OMA; IYDINWR; -.
DR   PhylomeDB; P29849; -.
DR   BioCyc; SPNE170187:G1FZB-2194-MON; -.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR   GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011833; Glycg_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   PANTHER; PTHR11468; PTHR11468; 1.
DR   Pfam; PF00343; Phosphorylase; 1.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   TIGRFAMs; TIGR02093; P_ylase; 1.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; Carbohydrate metabolism; Glycosyltransferase;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..752
FT                   /note="Maltodextrin phosphorylase"
FT                   /id="PRO_0000188562"
FT   MOD_RES         603
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        82..89
FT                   /note="GKDLIEVE -> ATPTTKGT (in Ref. 2; AAA26924)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   752 AA;  85202 MW;  BC3A15893EC4C4C0 CRC64;
     MLSLQEFVQN RYNKTIAECS NEELYLALLN YSKLASSQKP VNTGKKKVYY ISAEFLIGKL
     LSNNLINLGL YDDVKKELAA AGKDLIEVEE VELEPSLGNG GLGRLAACFI DSIATLGLNG
     DGVGLNYHFG LFQQVLKNNQ QETIPNAWLT EQNWLVRSSR SYQVPFADFT LTSTLYDIDV
     TGYETATKNR LRLFDLDSVD SSIIKDGINF DKTDIARNLT LFLYPDDSDR QGELLRIFQQ
     YFMVSNGAQL IIDEAIEKGS NLHDLADYAV VQINDTHPSM VIPELIRLLT ARGIDLDEAI
     SIVRSMTAYT NHTILAEALE KWPLEFLQEV VPHLVPIIEE LDRRVKAEYK DPAVQIIDES
     GRVHMAHMDI HYGYSVNGVA ALHTEILKNS ELKAFYDLYP EKFNNKTNGI TFRRWLMHAN
     PRLSHYLDEI LGDGWHHEAD ELEKLLSYED KAVVKEKLES IKAHNKRKLA RHLKEHQGVE
     INPNSIFDIQ IKRLHEYKRQ QMNALYVIHK YLDIKAGNIP ARPITIFFGG KAAPAYTIAQ
     DIIHLILCMS EVIANDPAVA PHLQVVMVEN YNVTAASFLI PACDISEQIS LASKEASGTG
     NMKFMLNGAL TLGTMDGANV EIAELVGEEN IYIFGEDSET VIDLYAKAAY KSSEFYAREA
     IKPLVDFIVS DAVLAAGNKE RLERFYNELI NKDWFMTLLD LEDYIKVKEQ MLADYEDRDA
     WLDKVIVNIS KAGFFSSDRT IAQYNEDIWH LN