ID A0A0A2TEU2_9BACI Unreviewed; 812 AA.
AC A0A0A2TEU2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, 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=N782_11260 {ECO:0000313|EMBL:KGP72636.1};
OS Pontibacillus yanchengensis Y32.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385514 {ECO:0000313|EMBL:KGP72636.1, ECO:0000313|Proteomes:UP000030147};
RN [1] {ECO:0000313|EMBL:KGP72636.1, ECO:0000313|Proteomes:UP000030147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y32 {ECO:0000313|EMBL:KGP72636.1,
RC ECO:0000313|Proteomes:UP000030147};
RX PubMed=26561516; DOI=10.1186/s40793-015-0085-y;
RA Huang J., Qiao Z.X., Tang J.W., Wang G.;
RT "High quality draft genome sequence of the moderately halophilic bacterium
RT Pontibacillus yanchengensis Y32(T) and comparison among Pontibacillus
RT genomes.";
RL Stand. Genomic Sci. 10:93-93(2015).
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:KGP72636.1}.
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DR EMBL; AVBF01000026; KGP72636.1; -; Genomic_DNA.
DR RefSeq; WP_036819465.1; NZ_AVBF01000026.1.
DR AlphaFoldDB; A0A0A2TEU2; -.
DR STRING; 1385514.N782_11260; -.
DR eggNOG; COG0058; Bacteria.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000030147; 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:UP000030147};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 656
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 812 AA; 93377 MW; 51602D8FD28379C6 CRC64;
MFSEKEEFKK AFSRKLQAEL GVHVENATEF DVYRALGSLV QDKIGEDWLQ TQQQYKNKKE
KQVYYFSMEF LMGRLLGNNL LNLQVLQMVE EGLSDYGFSL SRIEDQEHDA GLGNGGLGRL
AACFLDSLAS LELPGHGCGL RYRYGMFDQR FMNGYQVELP DNWLSDQFIW EVRRPEEAIE
VKFGGHVSTT NNKSGELSFR YKDYNTLRAV PYDVPVVGYN NEVVNTLRLW SAEPTENDVL
TVAKQQNDFT NMLDHQRSLE SISDFLYPDD STEEGKTLRL KQEYFLVSAG VQSAVRQFEQ
LELPWSSFSN QVALHINDTH PALVIPELMR ILLDEKELGW EEAWEITQST VSYTNHTTLS
EALETWPVDL VRNLLPRIFM IIEEMNERFC QSLWKTYPGD FDRIASLAII ADGQVKMAHL
SIVGSHSING VAKLHTEILK KREMKTFYET FPNRFTNKTN GITHRRWLMH ANRPLSQLIS
DQIGEQWKED PEQLTNLLTK QEDTSLLDSL YDVKQQKKDA FADWVHKETG IMVDPSSIFD
VHIKRLHGYK RQLLNALHIM HLYNEIKSGH AKNMVPRTFF FGAKAAPGYH FAKKVIKLIN
RISDVVNNDS DVNDKLNVVF LENYSVSLAE RIIPAANISE QISTASKEAS GTGNMKLMMN
GALTLGTLDG ANIEINEVVG DENMYTFGLR SNEVLRFYKE GGYSSKEVYD ADARIRHTLD
QLIHYSPFSK GETEFRDLYD ALLTYNDEFF VLKDFASYVE AQQQINEDYK QTREWSKRSL
INIAHSGKFS SDQTIQSYAS DIWRLQPVKT LR
//
