ID A1AR77_PELPD Unreviewed; 829 AA.
AC A1AR77;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN OrderedLocusNames=Ppro_2240 {ECO:0000313|EMBL:ABK99847.1};
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABK99847.1, ECO:0000313|Proteomes:UP000006732};
RN [1] {ECO:0000313|EMBL:ABK99847.1, ECO:0000313|Proteomes:UP000006732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC {ECO:0000313|Proteomes:UP000006732};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
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 ECO:0000256|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; CP000482; ABK99847.1; -; Genomic_DNA.
DR RefSeq; WP_011736108.1; NC_008609.1.
DR AlphaFoldDB; A1AR77; -.
DR STRING; 338966.Ppro_2240; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; ppd:Ppro_2240; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_7; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000006732; 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 CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 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 ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006732};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 669
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 829 AA; 94994 MW; 935BB11E1B23F711 CRC64;
MNAPDNSTQA DAKPTPSDLQ RSFLRHLKHT IVKDKYSATP ADLYLALAYA VRDMLAERWL
ETQQAYYRNN AKRVYYISME FLMGRTLGNS LINLGIMEEW EGALKQLGID ATDLQESEWD
AGLGNGGLGR LAACFLDSLA TMSLPAYGYG IRFEYGMFFQ KIVDGGQYET PDNWLRYGNP
WEFGRQEHLH KIRYHGRVTE YRDEEGMQRH DWVDTHDVMA MAYDVPVPGY GNETVNTLRL
WSAKSTRDFE LSFFNQGNYI GAVESKMRTE NISKVLYPAD HMAEGKELRL RQEYFLSSAT
VQDIFYRFSK KHGDVSILPT KVAIQLNDTH PTLAIPELVR ILLDEKLLAW DDAWKISVET
FAYTNHTVLP EALETWPVRI LENILPRHLQ IIYQINDHFL REVASRFPDD MERLRRMSIV
AEEGEKHIRM AHLAIVGSHS VNGVSALHSQ ILKDDLFHDF YEMWPERFNN KTNGITQRRW
LKHANRWLAD LVSSRIGHGW ITDLGELARL RELADDREFQ QQWIEVKQAN KRHLADLILR
DTGVRVSADS LFDCQTKRIH EYKRQLLNVL HVITRYNRIK ATPGCAITPR TVIFSGKAAP
SYFMAKLIIQ LITAVGAVVN NDPAIHGLLK VVFMPNYNVS LAECIFPAAD LSEQISTAGT
EASGTGNMKY ALNGALTIGT LDGANIEIME EVGRDNIFIF GLTSKQVTHL KRAGYHPRDH
YLSDPELKQA LDMIAGGTFS PDDPDRFRPI SDNLLANDHY LLLADYASYI TSQEQVDRLY
QEPYEWARRS ILNTAGMGKF SSDRTIAEYA REIWNIQPEI IRPTRRFNI
//
