ID A0A087A0A4_9BIFI Unreviewed; 818 AA.
AC A0A087A0A4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=BBIA_0498 {ECO:0000313|EMBL:KFI52204.1};
OS Bifidobacterium biavatii DSM 23969.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437608 {ECO:0000313|EMBL:KFI52204.1, ECO:0000313|Proteomes:UP000029108};
RN [1] {ECO:0000313|EMBL:KFI52204.1, ECO:0000313|Proteomes:UP000029108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23969 {ECO:0000313|EMBL:KFI52204.1,
RC ECO:0000313|Proteomes:UP000029108};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFI52204.1}.
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DR EMBL; JGYN01000006; KFI52204.1; -; Genomic_DNA.
DR RefSeq; WP_033492782.1; NZ_JGYN01000006.1.
DR AlphaFoldDB; A0A087A0A4; -.
DR STRING; 1437608.GCA_000771645_02121; -.
DR eggNOG; COG0058; Bacteria.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000029108; 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:UP000029108};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 667
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 818 AA; 92155 MW; 3AB06A9B9B07F235 CRC64;
MTEITAPKSP VTTEEFTDRI REQLKYAQGV TPEQATPADV YVASSLVVRH YLQDAWFKTQ
QDMVNGNTKA VGYLSAEFLM GKQLRNALLN AGMIDQFDAA VEGLGFKPQD VIDAEYEPAL
GNGGLGRLAA CFIDSLASLG VPAFGYGIQY RYGIFKQEFD KDGKQVEKPE YWLANEEPWG
HTDYNRSQRV NFGGKVVTKA DGSKEWQPEW SVRAVPVDYM VPGYASGRVN TLRLWTAKSY
DEFDLATFNK SDYLNAVKPK VKAEDISKIL YPEDSTPQGK ALRLEQQYFF VSASIHDAIR
VFYPGQDKPD LTTFPDKITF QLNDTHPVIG IPELMRVLID EYGYDWNTAW DITTRTFNYT
CHTLLPEALE VWPAKLIGEL LPRHLEIIKA INTNFLAELA TKTRDKAKID RMRIVTEGDN
PQVRMAYLAT AGGSHVNGVA ALHSELLKDV TLRDFSDIYP DKFTNVTNGV TPRRFIRLAN
PRLSALITEG LGTDRWLSDL ELLKGLEPLA KDDEFVKKFA AVKQANKEDF AAYAKREYGF
ELDPNTMFNT MVKRLHEYKR QSLKILALIA KYADIKSGKV NVDDVLPRTV IFGAKAAPGY
YLAKMTIQLI NNVARVVNND PDVKGKLNVY FPWNYNVRLA QHLIPATDLD EQISQAGKEA
SGTGNMKFAL NGAMTVGTLD GANVEIRERV GAENFFLFGM TVDEVDKLYE EGYSPAKYYE
ADPRLKAAID MVSDGTFSNG DRNTYAPLVA DWLTKDWFMT LADFTAYTEI QSDIEALYRQ
PLEWNRKALL NVANSGYFSS DRSITDYLER IWHTGPLA
//
