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Database: UniProt
Entry: R5ZTU7_9BACT
LinkDB: R5ZTU7_9BACT
Original site: R5ZTU7_9BACT 
ID   R5ZTU7_9BACT            Unreviewed;       876 AA.
AC   R5ZTU7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Maltodextrin phosphorylase {ECO:0000313|EMBL:CDA42843.1};
GN   ORFNames=BN693_01009 {ECO:0000313|EMBL:CDA42843.1};
OS   Prevotella sp. CAG:5226.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262930 {ECO:0000313|EMBL:CDA42843.1, ECO:0000313|Proteomes:UP000018184};
RN   [1] {ECO:0000313|EMBL:CDA42843.1, ECO:0000313|Proteomes:UP000018184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:5226 {ECO:0000313|Proteomes:UP000018184};
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:CDA42843.1}.
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DR   EMBL; CBBW010000073; CDA42843.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5ZTU7; -.
DR   Proteomes; UP000018184; 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; 2.
DR   InterPro; IPR011834; Agluc_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR   NCBIfam; TIGR02094; more_P_ylases; 2.
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; 2.
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:UP000018184}.
FT   DOMAIN          22..123
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
FT   MOD_RES         631
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   876 AA;  100989 MW;  E40FF35057858427 CRC64;
     MNIKISNANQ PSWKVINVKS HIPEALKKLD ELAHNLWWSW NTEAMQLFAS LDEDLWKKVN
     KNPIDLLCSI DYDRLIELSK DGETIARMDK VYGDFRKYMD VKPDAKRASV AYFCMEYGLN
     HVLKIYSGGL GVLAGDYLKE ASDSNVDLVA VGFLYRYGYF TQSLSMDGQQ IANYEAQDFD
     RLPIERVLDK DGNQVIVNVP YPNFMVHAAL WVANVGRIKL YLLDTDNDMN SEFDRRITHS
     LYGGDWENRI KQEYLLGIGG MLALKQLGIK KDIYHCNEGH AALCNVQRLA EYVESGMTFD
     EALELVRASS LYTVHTPVPA GHDYFDEGLF NKYMNQFPAR LGISWDEFMG LGRTNPDDKG
     EKFCMSTFLC KTCQEVNGVS WLHGRVSQQM FKDIWPGYLP SYTHPNHTER SHDEWFKIYN
     PHPEESHVGY VTNGVHFPTW CAKEWQAVYA KYLGKDYIYD QSNSKIWEKI YNVPDEVIWN
     TRVLLKNKLI DYIRARFREN WLRNQGDPSL VVSLLDKINP NALLIGFARR FATYKRAHLL
     FSDLDRLSKI VNNPDYPVQF LFAGKAHPAD GAGQGLIKKI YDISQRPEFM GKILFLDNYD
     MQLARRLVSG VDIWMNTPTR PLEASGTSGE KALMNGVINL SVLDGWWYEG YREGAGWALT
     DRRTYENQEH QDKLDASTIY SMLEQEIIPL YYARNRKGYS ENWVRTVKNS IACIAPQYTM
     KRQLDDYYDR FYNPEAARFK TLTAHDNQLA KDIASWKESV AQRWDNIRVV SSERSENLQN
     GALVSGKEFS VKHVIDEQGL DDAIGVDLVI MSGAEGSEEI YTVMPMNVVG REGNLYTFEL
     TSSVDLAGSY KVAYRMYPKN KNLPNRQDFC YVRWFI
//
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