ID A0A0D6B2V4_RHOSU Unreviewed; 792 AA.
AC A0A0D6B2V4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=NHU_01869 {ECO:0000313|EMBL:BAQ69024.1};
OS Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=35806 {ECO:0000313|EMBL:BAQ69024.1, ECO:0000313|Proteomes:UP000064912};
RN [1] {ECO:0000313|EMBL:BAQ69024.1, ECO:0000313|Proteomes:UP000064912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2351 {ECO:0000313|EMBL:BAQ69024.1,
RC ECO:0000313|Proteomes:UP000064912};
RA Nagao N.;
RT "Genome sequene of Rhodovulum sulfidophilum DSM 2351.";
RL Submitted (FEB-2015) 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; AP014800; BAQ69024.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D6B2V4; -.
DR KEGG; rsu:NHU_01869; -.
DR PATRIC; fig|35806.4.peg.1926; -.
DR eggNOG; COG0058; Bacteria.
DR Proteomes; UP000064912; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 639
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 792 AA; 88173 MW; 233706CDCE46041A CRC64;
MTAADMRDSI LRHLAYELGT DPGHATLHDW RIALSLAVRD RLVDRWFAAN RATRAAQPKR
VYYLSMEFLI GRLLEDAIVN LRLEEQAGTA LADLGLDFDA VIQNEPDAAL GNGGLGRLAA
CFMESLATIG CPAFGYGIRY ENGLFRQSFQ DGRQIEEPED WLSQFHAWEF ERRDVAQEIR
FGGEVTQKDG RAVWTGAEAV IAAAFDTPII GWKGRWANTL RLWSAQPLHG FDLARFNRGE
YAAAAEPEAL ARTISRVLYP DDTTGQGKEL RLKQEYFFTA ASLRDILRRF EAEGGALADL
PKKAAIQLND THPAIAGPEL VRLLHDERGM ALDQAIATAR GCLSYTNHTL MPEALERWSE
DLMSQLLPRH MQLIERIDEA HAAEMPGRRV TLRENGEVKM GEIAFTMAHK VNGVSALHTD
LMKETVFADL HRLHPDRIVN ETNGVTPRRW LLSANPRLSR LITETIGEGW VDDLEQLDRL
EASISDPGFL DAYAKAKREN KQDFAEWLAA EQGVRVDPEA LFDVQIKRIH EYKRQHLNIL
ETVALWREIK ANPGAGWVPR VKIFAGKAAP GYVFAKEIIH LINDVAEVLN ADPVTSPYLK
VLFLPNYNVS LAERLIPAAD LSEQISTAGK EASGTGNMKF ALNGAPTIGT LDGANVEIRD
RVGARNFFLF GMTAQEVEAR RAVPDHARQA IQADPRLGGA LTAISQGAFS PSDKHRYRGV
VANLTGQDYF LVCSDFTAYW DAQRRAEAAF ADPAVWHRIA ACNTARAGWF SSDRTIRGYM
TDIWGTVPLA AE
//
