ID W5TFQ3_9NOCA Unreviewed; 860 AA.
AC W5TFQ3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN Name=glgP {ECO:0000313|EMBL:AHH16081.1};
GN ORFNames=NONO_c12780 {ECO:0000313|EMBL:AHH16081.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH16081.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH16081.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH16081.1};
RX PubMed=24747905;
RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT Analysis of the Complete Genome of Nocardia nova SH22a.";
RL Appl. Environ. Microbiol. 80:3895-3907(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; CP006850; AHH16081.1; -; Genomic_DNA.
DR RefSeq; WP_025347602.1; NZ_CP006850.1.
DR AlphaFoldDB; W5TFQ3; -.
DR STRING; 1415166.NONO_c12780; -.
DR KEGG; nno:NONO_c12780; -.
DR PATRIC; fig|1415166.3.peg.1298; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_11; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000019150; 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 ECO:0000313|EMBL:AHH16081.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019150};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AHH16081.1}.
FT DOMAIN 13..124
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 614
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 860 AA; 94742 MW; 6D34DE846A1C082A CRC64;
MKALRRFTVR AHLPQRLTAL GELAANLRWS WHGPTQDVFA RLDPELWVRV GRDPVRMLGE
VPADRLDEWA ADPDYAADVD AAAADLRDYL SRPRWYGEYA ATSETPVPGG IAYFSMEFGV
TEVLPNYSGG LGILAGDHLK AASDLGLPLI GVGLLYRSGY FRQSLTADGW QAERYPDLDP
QGLPLRLLAQ EGAPVLVHVP MPEGRVLRAQ VWIAQVGRIP LLLLDSDIAD NDPELRAVTD
RLYGGDQDHR IKQEILAGIG GVRAVRAYTR ARGLPDPDVW HMNEGHAGFL GIERIREYIS
GGMDFDSALT AVRAATVFTT HTPVPAGIDR FAAALVRRYF GGTHGDRESP LLPGISVDRI
LALGREADPS VFNMAHLGLR LAQRANGVSK LHGEVSRAMF APLWPGFDVA EVPIGSVTNG
VHAPTWAARE WIDTARELVG PELVAEARGW EQLREVDPHE LWATRTTLRA VLVDEVRRRV
RASWLERGAA PAELGWVDQV FDPDVLTVGF ARRVPTYKRL TLMLRDPDRL RALLLDPVRP
VQLVVAGKSH PADEGGKALI QQVVRFADDP AVRHRIVFLP DYDMSMARYL YWGCDVWLNN
PLRPLEACGT SGMKAALNGG LNLSIRDGWW DEMYDGDNGW AIPTADGVRD ENRRDDLEAS
ALYEMLERSV LPHFYDRDDT GLPVRWLEMV RHTLRTLGPK VLASRMVRDY TTGYYFPAAA
SYAAVAAEDF AGARELAEFR RRADSAWPQV KVVRVDSSGL PDIPVIGAEL SLRARIDLAG
LSPDEVEVQA VLGRVGADDE LVDTAVAEMS HVATDSGTEL YEVTTPVPRS GAVGYTVRIL
PRHRLLSGAA ELGLVAAASP
//
