ID A6UD39_SINMW Unreviewed; 821 AA.
AC A6UD39;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN OrderedLocusNames=Smed_2739 {ECO:0000313|EMBL:ABR61569.1};
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394 {ECO:0000313|EMBL:ABR61569.1, ECO:0000313|Proteomes:UP000001108};
RN [1] {ECO:0000313|Proteomes:UP000001108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419 {ECO:0000313|Proteomes:UP000001108};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABR61569.1, ECO:0000313|Proteomes:UP000001108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419 {ECO:0000313|EMBL:ABR61569.1,
RC ECO:0000313|Proteomes:UP000001108};
RX PubMed=21304680; DOI=10.4056/sigs.43526;
RA Reeve W., Chain P., O'Hara G., Ardley J., Nandesena K., Brau L., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Hauser L., Chang Y.J., Ivanova N., Mavromatis K., Markowitz V.,
RA Kyrpides N., Gollagher M., Yates R., Dilworth M., Howieson J.;
RT "Complete genome sequence of the Medicago microsymbiont Ensifer
RT (Sinorhizobium) medicae strain WSM419.";
RL Stand. Genomic Sci. 2:77-86(2010).
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; CP000738; ABR61569.1; -; Genomic_DNA.
DR RefSeq; YP_001328404.1; NC_009636.1.
DR AlphaFoldDB; A6UD39; -.
DR STRING; 366394.Smed_2739; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; smd:Smed_2739; -.
DR PATRIC; fig|366394.8.peg.5944; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_5; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000001108; 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 REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 673
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 821 AA; 92353 MW; 5DBB507341CFADCD CRC64;
MMNRLSNTEL PQPAPRSSEP SQLAVEILER LKYRIGKDPK VAKPHDWLTA AILVARDRIT
DKWMDSTRKT YSTGAKRVYY MSLEFLIGRM MRDAMTNLGL MDEMRDALAS LGVDIDVIAA
LEPDAALGNG GLGRLAACFM ESMATVDVPA YGYGIRYMHG LFRQQMADGW QVELPETWLA
HGNPWEFERR ECSYEIGYGG SVETVNIDEE VQRYVWKPAE RVIATAFDTP AVGWRATRVN
TLRLWAAQPI DPILLDAFNA GDHIGALRES NKAESLTRVL YPADATPAGQ ELRLRQEYFF
SSASLQDILR RHLQQYPDFT SLPDAVAIQL NDTHPAVSVA ELVRLLSDVH GLDFEQSWDI
ARRTFSYTNH TLLPEALESW PVPLFERLLP RHMQIVYAIN AKILIEARRV RYATDEAIRN
ISLIDETGER RVRMGNLAFV GSHSINGVSA LHTELMKETV FADLHALYPD RINNKTNGIT
PRRWLMQCNP DLFGLIREAI GDEFIDNTEA LQALDAFADN ADFQERFAAV KRANKVRLAK
LIQANLGIRL DPSAMFDIQI KRIHEYKRQL LNLIEAVALY DQIRSHPELD WVPRVKLFAG
KAAPSYHNAK LIIKLANDIA RVINNDPAVR GLLKVVFIPN YNVSLAEVMV PAADLSEQIS
TAGMEASGTG NMKFALNGAL TIGTLDGANV EMRDWVGEEN IQIFGMTAED VGKARAEGHN
PRAIIENSRE LSQALSAIAS GVFSPDDRNR FSGLVDGLYN HDWFMVAADF EAYAKAQREI
DQLWTKPAAW YSKAVRNTAR MGWFSSDRTI RQYAGEIWRA G
//
