ID W5WRQ5_9PSEU Unreviewed; 853 AA.
AC W5WRQ5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=KALB_7502 {ECO:0000313|EMBL:AHI00860.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHI00860.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHI00860.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHI00860.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
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 {ECO:0000256|ARBA:ARBA00025174}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047}.
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DR EMBL; CP007155; AHI00860.1; -; Genomic_DNA.
DR AlphaFoldDB; W5WRQ5; -.
DR STRING; 1449976.KALB_7502; -.
DR KEGG; kal:KALB_7502; -.
DR PATRIC; fig|1449976.3.peg.7536; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_11; -.
DR Proteomes; UP000019225; 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 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 InterPro; IPR035090; Pyridoxal_P_attach_site.
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.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019225};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..129
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 611
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 853 AA; 93321 MW; 43506861FE462C8F CRC64;
MSPAVRALRR FTVRASLPEP LSALGQLATN LRWTWHPPTQ ELFAAVDAQA WEQAGNDPLR
LLRDVPAAHL ERLAADESFL TRTRAVAEDL NRYLTEPRWY QRRQQDADQT RLPASIGYFS
MEFGVTEALP NYSGGLGVLA GDHLKAASDL GVPLIGVGLL YRSGYFRQSL SLDGWQVEHY
PVLDPRGLPL ELLTEPSGAP ILVHVALPGG RVLRARIWKA QVGRVPLLLL DSNVEDNDPD
LRGVTDRLYG GDQDHRIQQE ILAGIGGVRA VRVYCELTGT AQPGVFHTNE GHAGFLGLER
IRELITGDGL DFDEALAAVR AGTVFTTHTP VPAGIDRFPV DLVQHYFGGE QLLPGVPIQR
VLALGAEENP GLFNMAHMGL RLAQRANGVS RLHGEVSRGM FGGLWQGFDA REVPIGSVTN
GVHGPTWAAG EMSKLLGGSE ADTGTGPLTF EPVTDSLLWE LRCGLRGKLV DEVRRRVRVA
WLQRGASALE LGWTDSVFDP DVLTVGFARR VPTYKRLTLM LRDPERLRAL LLHPERPVQL
VVAGKSHPAD DGGKALIQQI VRFADDAGVR HRIVFLPDYD MSMARYLYWG CDVWLNNPMR
PLEACGTSGM KAALNGGLNL SIRDGWWDEF YDGSNGWAIP TADGVADPNR RDDLEAAALY
ELLNQQVAPL FYDRGADGVP TRWMAMVRHT LASMGPNLQA SRMVREYVEN YYAPAGRSAG
SVRENSFQGA KELAVYRARI RAAWNRVHVV DTDMSVNGAQ APVVGHPVTV RARVDLNGLT
PADVDVQAVI GRVADSGELS EVVTESMRVD GDGSYVAEMP LPHVGSVGYT VRVLPKHELL
ATPAELGRVI LAG
//
