ID A5UEJ6_HAEIG Unreviewed; 821 AA.
AC A5UEJ6;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=glgA {ECO:0000313|EMBL:ABQ99201.1};
GN OrderedLocusNames=CGSHiGG_00460 {ECO:0000313|EMBL:ABQ99201.1};
OS Haemophilus influenzae (strain PittGG).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374931 {ECO:0000313|EMBL:ABQ99201.1, ECO:0000313|Proteomes:UP000001990};
RN [1] {ECO:0000313|EMBL:ABQ99201.1, ECO:0000313|Proteomes:UP000001990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PittGG {ECO:0000313|EMBL:ABQ99201.1,
RC ECO:0000313|Proteomes:UP000001990};
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
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; CP000672; ABQ99201.1; -; Genomic_DNA.
DR AlphaFoldDB; A5UEJ6; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; hiq:CGSHiGG_00460; -.
DR HOGENOM; CLU_010198_1_1_6; -.
DR Proteomes; UP000001990; 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 667
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 821 AA; 94479 MW; 9940C8B64057914A CRC64;
MIMDNFDSPF QYNRPEMTVE AIKKSIVYKL IFLIGRSPRE ASQRDWLNAT LHAVRDLVTE
GWITTARQTR AEDSRRVYYL SMEFLIGRTL SNAMIAEGIY GLAQEALSEL NVDLEEVLEK
EVDPGLGNGG LGRLAACFMD SIATLGLPGM GYGIRYEYGM FRQKIENGQQ VECPDAWLEK
GAPWEFIRPS KRFTVEFGGN IHFEGKKCIW QDTEKVTALA YDQMIPGYQN NSAATLRLWS
AHAGEVFNLA DFNRGEHLAA LEEHSANKNL SRVLYPDDST WNGRELRLRQ EYFLVSASLQ
DILRRHKRTH DSLENLADKV AIHLNDTHPA LAIPELMRIL VDDEGFEWKK AWEMTRNIFS
YTCHTLMSEA LETWPVEMMA KILPRHLQMI FEINDHFLEY VRTYVTTDND FIRRVSLIEE
GYQRKVRMGW LSVVGSHKIN GVAEIHSDLM VTSTFADFAR IFPERFTNVT NGITPRRWLA
VANPQLADLF DKYIGSEWRC DLSQIEKLKP FTQEKAFKEA IADIKFANKV KLAEYVKCEL
GVELDPHALF DVQVKRIHEY KRQMLNVLHI IARYNEMLVN PEKDWQPRVF ILAGKAASAY
YAAKQTIHLI NDVANVINND ERLKGRLKVV FIPNYSVSLA QLIIPAADIS EQISLAGTEA
SGTSNMKFAL NGALTLGTLD GANVEILENV GEDNIFIFGN TVEQVEQLRR EGYRSFEYYQ
NDAQLRTVVD QIIEGKFSPE EAQRYHQLLQ GLQYHDYYQA FADFRSYVET QKAVDEKYKQ
RDQWIESTIQ NIVNMGFFSS DRTIKEYAER IWKVEPVQLG D
//
