ID A0A0K9G9H3_9BACI Unreviewed; 805 AA.
AC A0A0K9G9H3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=AC622_03475 {ECO:0000313|EMBL:KMY43404.1};
OS Bacillus sp. FJAT-27916.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1679169 {ECO:0000313|EMBL:KMY43404.1, ECO:0000313|Proteomes:UP000036953};
RN [1] {ECO:0000313|Proteomes:UP000036953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27916 {ECO:0000313|Proteomes:UP000036953};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-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}.
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:KMY43404.1}.
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DR EMBL; LFZV01000001; KMY43404.1; -; Genomic_DNA.
DR RefSeq; WP_049669785.1; NZ_LFZV01000001.1.
DR AlphaFoldDB; A0A0K9G9H3; -.
DR STRING; 1679169.AC622_03475; -.
DR PATRIC; fig|1679169.3.peg.719; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000036953; 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:UP000036953};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 647
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 805 AA; 93255 MW; 2769B1A988B1D4BF CRC64;
MFDNKEQFKK AFLSKLEMSV GKSFEETSLQ DQYHVLGNMI REYISNNWIK TNQVYRTSET
KQVYYLSIEF LLGRIMGSNI LNLGIHDVVE EGLADLGINL EDLESTEPDS ALGNGGLGRL
AACFMDSLAS LDLPGHGCGI RYKYGLFEQK IIDGVQVEYP ELWLQNGQVW EVRKSDLAVE
VPFWGKVESY YDEDGRLCFK HRDAEPIMAV PYDIPVVGYH TETVNTLRLW NAEPANVPFH
DDIMRYKRET EMVSEFLYPD DAEDSGKILR LKQQYFLVRA SIDAILNTFR KKQKDIRQLP
DYVSIHINDT HPVLAIPELM RILLDEEMLS WEEAWDITVQ TFSYTNHTTL SEALEKWPVR
LFQPLLPRIY MIVQEINERF CKELWDKYPG QWQRIEDMAI IAHDQVKMAH LALVGTHSTN
GVAHLHTEIL KKREMNNFYQ VFPERFNNKT NGITHRRWLI KSNPALSNLI TESIGDKWMV
DPSCLKGVES FQNDAAFLEK LEKVKHDNKV KLAERIFQQN QIKVNVDSIF DVQVKRLHAY
KRQLLNVLHI MYLYNRMKEE PNFRPHPRTF IFGAKASPGY YYAKKIIKLI NTVAEKVNND
KTTNDYLKVV FLENYRVSLA EEIFPASEVS EQISTASKEA SGTGNMKFMM NGALTIGTMD
GANVEIHERV GKDNIFIFGM TSDEVMNYQA HGGYHSSEYY MLDRRIHEAV NQLVNGFFPN
TNGMFDMIYD SLLIENDQYF VLRDFDSYAK TQEMVSKAYE DKKKWNQSSV VNIANSGFFS
SDRTISEYAD NIWHIKPVNS PIIQA
//