ID W0QB43_9PAST Unreviewed; 789 AA.
AC W0QB43;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=X808_15940 {ECO:0000313|EMBL:AHG76114.1};
OS Mannheimia varigena USDA-ARS-USMARC-1296.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Mannheimia.
OX NCBI_TaxID=1433287 {ECO:0000313|EMBL:AHG76114.1, ECO:0000313|Proteomes:UP000066995};
RN [1] {ECO:0000313|EMBL:AHG76114.1, ECO:0000313|Proteomes:UP000066995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA-ARS-USMARC-1296 {ECO:0000313|EMBL:AHG76114.1,
RC ECO:0000313|Proteomes:UP000066995};
RA Harhay G.P., Clawson M.L., Murray R.W., Lubbers B.V., Heaton M.P.,
RA Chitko-Mckown C.G., Harhay D.M., Smith T.P.L.;
RT "Annotation of the Mannheimia varigena USDA-ARS-USMARC-1296 complete
RT genome.";
RL Submitted (DEC-2013) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP006943; AHG76114.1; -; Genomic_DNA.
DR RefSeq; WP_025217814.1; NZ_CP006943.1.
DR AlphaFoldDB; W0QB43; -.
DR STRING; 1433287.X808_15940; -.
DR KEGG; mvi:X808_15940; -.
DR PATRIC; fig|1433287.3.peg.1593; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_6; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000066995; 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:SF25; MALTODEXTRIN 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 641
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 789 AA; 90851 MW; AAEEF9C983C22157 CRC64;
MTFNSIVEKY CRYFDVADPK HFTLQQWYQV VAEGSLELIY SQPATKPTES RHVNYLSMEF
LIGRLTGNNL MNLGYYEQIR DYLKQYQVEL VDVLEQERDP ALGNGGLGRL AACFLDSMAT
VGQNATGYGL HYQYGLFKQS FKEGMQKEAP DTWARDSYPW HRFNPSKTRH IGFGGKIKQI
QADQYEWQPK LTIQGKAFDL PIVGYKNNII QPLRLWQADS DQSFDFDAFN DGKFLTADKT
IVNAAALTQV LYPNDNHKAG QKLRLMQQYF HCACSVADIL DRHLSEGYPL EDLAKRQVIQ
LNDTHPTLAI PELMRVLLDD HQFTWEQAWD ICSNTFAYTN HTLLPEALEQ WDQRLFKQLL
PRHYQIVEKI NDIFHNQVRA EFGDDAKIWE KLAVLFDYRV RMANLCVVTC FRVNGVAEIH
SNLLVTDLFP EYHRLFPTKF CNVTNGITPR RWIRQANPQL SDLLDRTLKQ DWTHDLELLK
GVEKYVDDTG FREEYQRIKR NNKVVLANEI HKTLGLNVNP SAIFDVQIKR FHEYKRQHLN
LLNIIATYQS LKANPNQDYT PRVFLFSGKA APGYYLAKNI IHAINNVADI INNDKQVNDK
LQVVFLPDYR VSLAEKIIPA ADVSEQISMA GKEASGTGNM KLALNGALTL GTLDGANVEI
AEMVGEENVF IFGHTVESVR ELLAKGYQPK TYYNQDPILK NAVDFLAKGK ASHGNKETFK
LMLDSLLERD PFLVFADFDS YRQTQEKIGI AYLDQEAWLR SAILNTARLG TFSSDRSIKD
YQQRIWLNR
//
