ID B8GUU6_THISH Unreviewed; 824 AA.
AC B8GUU6;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN OrderedLocusNames=Tgr7_0359 {ECO:0000313|EMBL:ACL71457.1};
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL71457.1, ECO:0000313|Proteomes:UP000002383};
RN [1] {ECO:0000313|EMBL:ACL71457.1, ECO:0000313|Proteomes:UP000002383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL71457.1,
RC ECO:0000313|Proteomes:UP000002383};
RX PubMed=21475584;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL71457.1; -; Genomic_DNA.
DR RefSeq; WP_012636946.1; NC_011901.1.
DR AlphaFoldDB; B8GUU6; -.
DR STRING; 396588.Tgr7_0359; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; tgr:Tgr7_0359; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_6; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000002383; 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:UP000002383};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 671
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 824 AA; 94659 MW; 263A79E0D59072EB CRC64;
MAAADILTEL EHHPRPCDKE GLKRSIRDAL IHQAGKDPLH ATPRDWLEAV SYAVRERLIE
RRMFTQRLFN QEHAKRVYYL SMEYLIGRML INSLMNLGFF DACREALSEM GVDLLEISEL
EPDAALGNGG LGRLAACILD SMASQCIPGY GYGIRYEYGM FQQQIQNGQQ IEHPDNWLRY
GNNWEFPRPE KIFPVRFYGR VVTHRDNGDV RHHWQDCEEV IAMAYDYPTP GYGNKNVNNL
RLWAAKATRD FDLNYFNEGD YIGAIQQKAE SETISMVLYP NDATAIGREL RLKQEYFFVS
ASIQDILSHH EEMGYRITEL ADKVAMQLND THPAIAVAEL MRLLLDKYQL PWVSAWEITR
AVFGYTNHTL MPEALETWPV ALMERVLPRH MQIIYEINFH FLNEVRHTFP GDTEIVKRLS
IIDEDHGRRV RMAHLAVVGS HHINGVAALH TQLLKDTLFH DFYRLWPERF ISITNGITPR
LWLNQANPAL TSMISEHIGK EWVMDLTQLR QLEAFAEDPT CRQEFRTVKE ANKRHLAELV
LERTGIEIDP AAMFDVQIKR IHEYKRQLLN ILHVIAFYNR IRHGEAPEQA QRVVLFAGKS
APAYVRAKQI IRLINDVADV INHDPVVEGR LKVVFYPNYD VSSAAVIIPA ADLSEQISTA
GMEASGTGNM KLALNGALTI GTLDGANVEI REAVGEENIF IFGLTTNEVA ETKARGYRPR
EHYEQNAELK EVIDMIASGF FSPSEPGRYR DLVHDLLNND AFLVLADFES YLHAQERVDA
LYRKPEEWTR RAMLNTARMG FFSIDRTVKQ YADEIWGVTP ECWI
//
