ID   PHSG_THELN              Reviewed;         831 AA.
AC   Q9YGA7; H3ZK82;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Maltodextrin phosphorylase;
DE            EC=2.4.1.1;
GN   Name=malP; ORFNames=OCC_08779;
OS   Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=523849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, INDUCTION, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX   PubMed=10348846; DOI=10.1128/jb.181.11.3358-3367.1999;
RA   Xavier K.B., Peist R., Kossmann M., Boos W., Santos H.;
RT   "Maltose metabolism in the hyperthermophilic archaeon Thermococcus
RT   litoralis: purification and characterization of key enzymes.";
RL   J. Bacteriol. 181:3358-3367(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX   PubMed=22493191; DOI=10.1128/jb.00123-12;
RA   Gardner A.F., Kumar S., Perler F.B.;
RT   "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT   litoralis NS-C.";
RL   J. Bacteriol. 194:2375-2376(2012).
CC   -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC       carbohydrate metabolism. Catalyzes the phospholytic cleavage of
CC       maltodextrins with a minimal chain length of five glucose residues to
CC       yield glucose-1-phosphate. Low activity with tetraose and no activity
CC       with triose and maltose. Long maltodextrins (8 to 15 glucose units),
CC       amylose and starch are not as good substrates as maltoheptaose.
CC       {ECO:0000269|PubMed:10348846}.
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         Evidence={ECO:0000269|PubMed:10348846};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:10348846};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.46 mM for maltoheptaose (at 60 degrees Celsius)
CC         {ECO:0000269|PubMed:10348846};
CC         Vmax=66 umol/min/mg enzyme with maltoheptaose as substrate
CC         {ECO:0000269|PubMed:10348846};
CC       Temperature dependence:
CC         Optimum temperature is 98 degrees Celsius.
CC         {ECO:0000269|PubMed:10348846};
CC   -!- SUBUNIT: Trimer (at 25 degrees Celsius). {ECO:0000269|PubMed:10348846}.
CC   -!- INDUCTION: Expressed constitutively. {ECO:0000269|PubMed:10348846}.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000305}.
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DR   EMBL; AF115479; AAD28735.1; -; Genomic_DNA.
DR   EMBL; CP006670; EHR79635.1; -; Genomic_DNA.
DR   RefSeq; WP_004066514.1; NC_022084.1.
DR   AlphaFoldDB; Q9YGA7; -.
DR   SMR; Q9YGA7; -.
DR   STRING; 523849.OCC_08779; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   PRIDE; Q9YGA7; -.
DR   EnsemblBacteria; EHR79635; EHR79635; OCC_08779.
DR   GeneID; 16550394; -.
DR   KEGG; tlt:OCC_08779; -.
DR   HOGENOM; CLU_015112_0_0_2; -.
DR   OMA; LYRHGYF; -.
DR   OrthoDB; 19755at2157; -.
DR   Proteomes; UP000015502; 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:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011834; Agluc_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   Pfam; PF11897; DUF3417; 1.
DR   Pfam; PF00343; Phosphorylase; 2.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   TIGRFAMs; TIGR02094; more_P_ylases; 1.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Carbohydrate metabolism; Direct protein sequencing;
KW   Glycosyltransferase; Maltose metabolism; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..831
FT                   /note="Maltodextrin phosphorylase"
FT                   /id="PRO_0000428945"
FT   MOD_RES         592
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   831 AA;  96683 MW;  80FBC5306BBA52ED CRC64;
     METVVNQIKS KLPENLEGLL DLAYNYWWSW NRRATKLWEK IDPEHWWEYK NPVKLLLDTP
     EERLKELSKD DDFINLYELV IDQFRHYMNP ESTWFSTNYP KWEEPVIYLC MEYGISKSLP
     IYSGGLGILA GDHIKTASDL GIPLIAIGLL YKHGYFKQEI DKDGKQIEVF PEYNPEEMPI
     KPLTTEKGKP LLIEVPIEDR IVYARAFEVN VGRVKLYLLD TDVPQNSPDD RTICDYLYNA
     EIDKRIKQEI LLGIGGMRLL RMLGIDPAVI HLNEGHPAFA NFQRIAWYME EGLNFLEALT
     VVRGTTIFTT HTPVPAGHDK FPIAEVEKRL AKFLEGLPKD EFLNLGREGD QFNMTLLSIR
     TSSYVNAVSK LHSKVTKEMW RHLWNGVPLD EIPVEGITNG VHTKTWLHNE IKKLVDRYIG
     RVWRDYAELE GLWYGVERIP DEELWEAHLK AKREFIELIK RKIKERNERL GIEEPLPEID
     ENALIIGFAR RFATYKRATL ILTDLERLKK IVNNPERPVY IIFGGKAHPR DEAGKEFLRK
     VYEVSQMPEF KNKIMVFENY DMGSARAMVA GVDVWLNNPR RPLEASGTSG MKAGLNGVLN
     LSVYDGWWVE GYNGKNGWVI GDESLEPETE KDNIRDAQSL YNLLENEVIP TYYENRARWI
     YMMKESIKSI APRFSTHRMV KEYVDKFYSK ALANAILLQR DSFKATREIA SWKAKIFNSW
     DKVEIERIIT HDATGVEVIV NLDGLSPEDV KVEIYYGVKA EGYAIEKPYV IELKHPQSLG
     GNRWLYRYEG NALKNLGHPC WHYAVRVYPY HDKLPHKFLL GLIKWKGFFE L