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Database: UniProt
Entry: R5PZL7_9BACT
LinkDB: R5PZL7_9BACT
Original site: R5PZL7_9BACT 
ID   R5PZL7_9BACT            Unreviewed;       851 AA.
AC   R5PZL7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:CCZ14327.1};
GN   ORFNames=BN679_01267 {ECO:0000313|EMBL:CCZ14327.1};
OS   Prevotella sp. CAG:487.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262928 {ECO:0000313|EMBL:CCZ14327.1, ECO:0000313|Proteomes:UP000018275};
RN   [1] {ECO:0000313|EMBL:CCZ14327.1, ECO:0000313|Proteomes:UP000018275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:487 {ECO:0000313|Proteomes:UP000018275};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001275};
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006047}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCZ14327.1}.
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DR   EMBL; CAZM010000176; CCZ14327.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5PZL7; -.
DR   Proteomes; UP000018275; Unassembled WGS sequence.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR   InterPro; IPR011834; Agluc_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR   NCBIfam; TIGR02094; more_P_ylases; 1.
DR   PANTHER; PTHR42655; GLYCOGEN PHOSPHORYLASE; 1.
DR   PANTHER; PTHR42655:SF1; GLYCOGEN PHOSPHORYLASE; 1.
DR   Pfam; PF11897; DUF3417; 1.
DR   Pfam; PF00343; Phosphorylase; 1.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018275}.
FT   DOMAIN          22..123
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
FT   MOD_RES         608
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   851 AA;  98522 MW;  9FFA38B7B5842547 CRC64;
     MKIKSDYANT PQWKELIVRS RLPEQLKCLD ELAHNMWWVW NYEAQELWKS LDEKLFEEVK
     HNPVLLLERL SYDRKEAIVK DHAIMSRVKS VYKKFREYMD VEPDHSRPSV AYFCMEYGLS
     HVLKIYSGGL GMLAGDYLKE ASDSNVDMCA VGFLYRYGYF IQSLNMDGQQ IAKYEAQNFE
     SLPIERENDA DGNPIVVDVP YMNYQVHAYV WRVNVGRIKL YLLDTDNELN SEFDKPITHS
     LYGGDNENRL KQEILLGIGG MLTLKKLGIK KDVYHCNEGH AALCNLQRLC DYVKSGLNFN
     QAMELVRASS LYTVHTPVPA GHDYFDESLF GKYMGGYPSM LGITWDEFIG MGRQNPDDHS
     EQFCMSVFAC NTCQEVNGVS KLHGWVSQKM FSPIWRGYYP EENHVGYVTN GVHFPTWTAP
     EWQKLYAKYF DKNFLNDQSN ESIWHGIYDV PDEEIWKTRM ILKKNLVDYI RKKFTETWLK
     NQGDPARVVS LLDRINPNAL MIGFCRRFAT YKRAHLLFTD IDRLAKIVNN PERPVQFIFS
     GKAHPADGAG QGLIKRVFEI SQRPEFLGKI IFLEDYDMQL ALRLVSGVDI WMNTPTRPLE
     ASGTSGEKAE MNGVVNLSVL DGWWVEGYRK GAGWALPQER TYQNQGYQDR LDAAMIYSLL
     ENDIAPLYYN RNKKGYSEGW IKTIKNSIAT IAPHYTMKRQ LDDYYSRFYT KQASLFKKLS
     ANDNQLAKEL AQWKETVAER WDSIHVVSKT DFVVSGVETG KKYSMQYVID EQGLNDAVGL
     EFVSVKTDLN GEERIFNVRE FKMVGHEGNL YTFELEFEPD VAGSFKGCVR MFPKNEMLAH
     RQAFCYVKWL D
//
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