ID K9SHU2_9CYAN Unreviewed; 861 AA.
AC K9SHU2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:AFY69339.1};
DE EC=2.4.1.1 {ECO:0000313|EMBL:AFY69339.1};
GN ORFNames=Pse7367_1041 {ECO:0000313|EMBL:AFY69339.1};
OS Pseudanabaena sp. PCC 7367.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=82654 {ECO:0000313|EMBL:AFY69339.1, ECO:0000313|Proteomes:UP000010386};
RN [1] {ECO:0000313|EMBL:AFY69339.1, ECO:0000313|Proteomes:UP000010386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7367 {ECO:0000313|EMBL:AFY69339.1,
RC ECO:0000313|Proteomes:UP000010386};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Pseudanabaena sp. PCC 7367.";
RL Submitted (MAY-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}.
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DR EMBL; CP003592; AFY69339.1; -; Genomic_DNA.
DR RefSeq; WP_015164312.1; NC_019701.1.
DR AlphaFoldDB; K9SHU2; -.
DR STRING; 82654.Pse7367_1041; -.
DR KEGG; pseu:Pse7367_1041; -.
DR PATRIC; fig|82654.3.peg.1205; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_3; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000010386; 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: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 Glycosyltransferase {ECO:0000313|EMBL:AFY69339.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010386};
KW Transferase {ECO:0000313|EMBL:AFY69339.1}.
FT DOMAIN 13..123
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 861 AA; 98359 MW; 813A6C6E15D358EE CRC64;
MRPIRTFNVK PSLPERLEPL RELAYNLYWS WSVEIRDLFR RLDPDLWDDT RHNPVLMLGT
ISQERLQEAL EDDGFLAQMD RAHQQLNDYL NKRTWYQKHR SGQAIEGECY AYYSAEFGLT
DCLPIYSGGL GILAGDHLKS SSDIGIPLVG VGLLYQKGYF KQYLNPDGWQ QERYPINDFY
NMPLHLERNP DGSELHISVD YPDESLGTKK VYARIWRIQV GMVKLYLLDT NIEPNNHTDQ
DITDYLYGGD IDVRIRQEMM LGIGGTRALV ALGYKPTAYH MNEGHAGFLS IARLEPLMQQ
EGLGYQEALQ LAQSTQIFTT HTPVPAGIDR FPPDKVWYYI GSYCDRLSIS KQQFLALGRE
HPEDEQEYFS MAVFAIKMAT YVNGVSKLHG AVSRDMFTRL WPQLPNAEVP ITSITNGVHA
RTWVSEDTQN LYDRYLGPSW SSGGVNDKLW ERVSTIPDEE LWRNHERQRA QLVLFARERL
KRQLTKWGAS PAEIKEAGEV LDPSALTVGF ARRFATYKRG TLFMYDRNRI KKLLKNSDRK
LQFVIAGKAH PKDTPGKELI RDIVRFSREE DVRHSIVFIE DYDTYVSGLM LAGCDIWLNT
PRRPREASGT SGMKAAMHGC LNLSILDGWW AEADYFNTGW PIGLGEEYDD HEYQNRIESN
AIYEILEKDA LPLFYHRSED GIPVGWLDKM KDSIRLNTPM FNTARMVRDY AQEAYIKASD
RMGELRTQNY GKAKHLAHWK ANLAQEWHAI TIKSVEVSTD ANDSTDVKVS QPIAVKAEIY
LAGLKPADVE VELYQGIVAE NGEVLDGKSY PMMLQSNSNG VSVYAAETSY GGSGLHGMSL
RILPKHPSLS SSYEPRLIHW A
//
