ID U7UTA9_9FIRM Unreviewed; 826 AA.
AC U7UTA9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=glgP {ECO:0000313|EMBL:ERT61678.1};
GN ORFNames=HMPREF1250_2091 {ECO:0000313|EMBL:ERT61678.1};
OS Megasphaera vaginalis.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1111454 {ECO:0000313|EMBL:ERT61678.1, ECO:0000313|Proteomes:UP000017090};
RN [1] {ECO:0000313|EMBL:ERT61678.1, ECO:0000313|Proteomes:UP000017090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BV3C16-1 {ECO:0000313|EMBL:ERT61678.1,
RC ECO:0000313|Proteomes:UP000017090};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (SEP-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERT61678.1}.
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DR EMBL; AWXA01000008; ERT61678.1; -; Genomic_DNA.
DR AlphaFoldDB; U7UTA9; -.
DR STRING; 1111454.HMPREF1250_2091; -.
DR PATRIC; fig|1111454.3.peg.423; -.
DR eggNOG; COG0058; Bacteria.
DR Proteomes; UP000017090; Unassembled WGS sequence.
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:UP000017090};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 674
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 826 AA; 95192 MW; E5D72E0E0B90BD58 CRC64;
MHRQMQGHLK RGLEREMKTW HTKEEFKSAF TKKAGILYDK ELHDLTRSEV YQIIAYMVRD
LVSDNWIRTN KAYVEKKTKQ IYYFSIEFLL GRLLESNLIG VDGEAVCREG LRDLGWELAD
ILPEERDPGL GNGGLGRLAA CFIDSLAALQ MPGHGCSLRY QYGLFKQKMV DDYQVELPDN
WLVNGFPWEV KRADKAVHVA FCGNAYMRPA DNGELECVYE GASYVRAVPY DVPIIGYRNN
TVNTLRLWRA EYSRDDVYRE LSLGDRHQAF LYKDSVQRIS RFLYPDDSTE DGRRLRLMQE
YFMVSAGVQS IIRHYKKKYK APLTAFADYM GIHINDTHPA LVIPELMRIF MDEEGLSWNQ
AWQITVRTVA YTNHTVLPEA LERWSIPMFK SLLPRIYLIL EELNERWLKK VRTLYPGDEG
KARDVAVLWG GQVHMAHLAV LGSHSTNGVA EIHSQILKDS TLHQLYTCFP SRFGNKTNGI
SHRRWLIQAN PQLAALLDDT IGTDWHGSPE RLEELMAYCN DASFLERLDG VKRERKRILG
SYLLKQYGVS VDVDSIFDVQ IKRIHLYKRQ LLNILHILHL YRRLKDDPSL VIAPRTYFFG
GKAAASYDEA KQTIRLISIV SRMINDDRRI SKMLRVMFLE NYNVSLGQIL FPAADVSEQI
STAGKEASGT GNMKFMMNGA LTLGTMDGAN IEIRRRVGDE NCVIFGLRAD AVMNYYIHGG
YSSWEVYSSD ENIRKVMDSL INGSIGDHEI FGMLYESLLD RNDEYFVLKD FEAYCGGQRE
IVRRYKNRRS WLHSSAVNIA QSGYFSSDRT IRQYAADIWH IQGVKV
//
