ID A0A168MYI9_9BACL Unreviewed; 804 AA.
AC A0A168MYI9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=PBAT_14755 {ECO:0000313|EMBL:OAB45194.1};
OS Paenibacillus antarcticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=253703 {ECO:0000313|EMBL:OAB45194.1, ECO:0000313|Proteomes:UP000077355};
RN [1] {ECO:0000313|EMBL:OAB45194.1, ECO:0000313|Proteomes:UP000077355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5836 {ECO:0000313|EMBL:OAB45194.1,
RC ECO:0000313|Proteomes:UP000077355};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Paenibacillus antarcticus CECT 5836.";
RL Submitted (MAR-2016) 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:OAB45194.1}.
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DR EMBL; LVJI01000018; OAB45194.1; -; Genomic_DNA.
DR RefSeq; WP_068650705.1; NZ_LVJI01000018.1.
DR AlphaFoldDB; A0A168MYI9; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000077355; 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:UP000077355};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 653
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 804 AA; 92740 MW; 0B4CC579DCDE320C CRC64;
MFSNKEAFKQ LFQENLVSKL GKPMKEAHKG DIYTVLSSMI REYAGENWAD TNQYFQSNQE
KQVYYFSMEF LIGRLLGNNL LNLGALELVR EGLKELGWDL EEIEEEESDA GLGNGGLGRL
AACFLDSLAS QRYAGHGCGI RYRYGLFEQK IVEGNQVELP DYWLRNGNEW EVRRPDKKVE
VRFWGNVEIR EEEKELVFET HNYETVTAIP YDVPVIGYGG EHVNTLRIWS AESTMDYTQI
SGTNNYYKFL DYNRSVESIS EFLYPDDSQY EGKLLRLKQQ YFLCSAGLQS ILRTFEKLEL
NIDHLPEKVA IHINDTHPTL VIPELMRILI DVVGLGWAQA WDITSRTVSY TNHTTLSEAL
EKWPISMVKE LLPRIYMIIE EINKQFCGML MKKYPGQPEI VAQMSIIDGQ QLKMANLAIV
GSYSVNGVAA LHTDILKKRE MKPFYNLYPH RFNNKTNGIT HRRWMMHANP MLAELISETI
STGWMNDPQE MTGILKYSED RGFQDRIHTI KQHNKLKLTS YIHEKQGIVV DPYSIFDIQV
KRLHGYKRQL MNVLHIMYLY TQLKQTPSMD IIPRTFIFGA KAAPSYSLAK RIIKLINVVA
DQVNRDREVN QKLQVIFLEN YSVSIAEKII PAADVSEQIS TASKEASGTG NMKFMMNGAL
TLGTMDGANV EMHEMIGDDN MFLFGLRSEQ VLDYYQHGGY AVKDVYDNDA RVSEVMDQLV
TSGYFCINEH EFGDIFDSIM STNDEYFVLK DFASYIETHK KIDISYRNSK EWQRKSIVNI
AHSGKFTSDY TIRKYASEIW GIRN
//
