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Database: UniProt
Entry: A0A0K9G9H3_9BACI
LinkDB: A0A0K9G9H3_9BACI
Original site: A0A0K9G9H3_9BACI 
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
//
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