ID C5C1X9_BEUC1 Unreviewed; 871 AA.
AC C5C1X9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN OrderedLocusNames=Bcav_1338 {ECO:0000313|EMBL:ACQ79597.1};
OS Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC Beutenbergia.
OX NCBI_TaxID=471853 {ECO:0000313|EMBL:ACQ79597.1, ECO:0000313|Proteomes:UP000007962};
RN [1] {ECO:0000313|EMBL:ACQ79597.1, ECO:0000313|Proteomes:UP000007962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432
RC {ECO:0000313|Proteomes:UP000007962};
RX PubMed=21304633; DOI=10.4056/sigs.1162;
RA Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT 0122).";
RL Stand. Genomic Sci. 1:21-28(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001618; ACQ79597.1; -; Genomic_DNA.
DR RefSeq; WP_015881837.1; NC_012669.1.
DR AlphaFoldDB; C5C1X9; -.
DR STRING; 471853.Bcav_1338; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; bcv:Bcav_1338; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_11; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000007962; 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; 2.
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:ACQ79597.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007962};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACQ79597.1}.
FT DOMAIN 13..133
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 625
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 871 AA; 94103 MW; 4DCCCD5354AFFE6A CRC64;
MRAFRRFTVR TVLPEPLAPL DELARNLRWS WHAPTRELFA SIDPQAWAAV RSDPVALLGA
VSPERLAALA ADPDVVARVH AAADDLRAYL TMPRWYQSLA PEGADGSSGA DRGDGPPRAI
AYFSAEFGIT AVLPQYSGGL GILAGDHLKS ASDLGVPIVG VGLLYGAGYF KQSLTRDGWQ
HETYPVLDPD NLPLTALRED DGTLATIEVP LPGGRTLRAQ VWRADVGRVP LLLLDSNVAG
NDDAARRVTD RLYGGTSEHR LQQELLLGIG GVRALRLFSR LTGAPEPEVY HANEGHAGFL
GVERIREIVE LEGTSFAAAR EAVRAGTVFT THTPVPAGID RFGVDLVRSY LGGASELPGV
PVDEVLALGA EDYDGGDPTV FNMAVMGLRL AKRANGVSLL HGAVSREMFS VLWPGFDAAE
VPIASVTNGV HGPTWTDPEF AGAAQEQFGA DAASGAGWLR GEDAGGVSDG RLWSERGRMR
ARLVHDARER VRRSWSDRGA SPAELGWVDD VLDPDVLTIG FARRVPTYKR LTLMLRDPER
LTRLLLDPDR PIQIVVAGKS HPADEQGVGL IQKFVQFADD ERVRERIVFL PNYDIAMAQV
LMPGCDVWLN NPLRPLEASG TSGMKCALNG ALNLSILDGW WDEWFDGQNG WAIPTADGVE
DPERRDDLEA AALYELLEGT VVPRFYDRDA DGLPRHWLEM VRHTLATLGP KVQATRMVAD
YVEQLYAPTA LDARAMDGTG HAGAVALAAW KERVRAGWPA VRVDHVETEG ADQAPRVGDA
VTVRAFVSLG DLAPSDVDVQ VTYGRVGEND ELTSFGTLSL AHTESYEAGR HQFSATVALE
RPGAFGYGVR VVPRHEGLAG ATELGLVVNA A
//
