ID A0A087DTT2_9BIFI Unreviewed; 818 AA.
AC A0A087DTT2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=BISU_2133 {ECO:0000313|EMBL:KFI98932.1};
OS Bifidobacterium subtile.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=77635 {ECO:0000313|EMBL:KFI98932.1, ECO:0000313|Proteomes:UP000029055};
RN [1] {ECO:0000313|EMBL:KFI98932.1, ECO:0000313|Proteomes:UP000029055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11597 {ECO:0000313|EMBL:KFI98932.1,
RC ECO:0000313|Proteomes:UP000029055};
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:KFI98932.1}.
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DR EMBL; JGZR01000016; KFI98932.1; -; Genomic_DNA.
DR RefSeq; WP_024463840.1; NZ_JGZR01000016.1.
DR AlphaFoldDB; A0A087DTT2; -.
DR STRING; 77635.BISU_2133; -.
DR eggNOG; COG0058; Bacteria.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000029055; 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:UP000029055};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 666
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 818 AA; 91569 MW; BEFBD0E076BA9E44 CRC64;
MTEHTAPMSS TTPGEFADEI RKELKYTQGV TTEQATSADV YVATATAVRK HLVDSWATTQ
HDMVAGSTKA VGYFSAEFLM GKQLLNALLN AGLSDQFYDA VKELGFDVQD VIDSEYEPGL
GNGGLGRLAA CYIDSLASKG VPAFGYGIQY RYGIFKQEFD EQGAQVERPD YWLANEEPWG
HIDYNRSQRV NYGGSVVEED GKKVWKPAWS VRAVPVDYMV PGYASGRVNT LRLWSAKSYD
EFDLLAFNKS EYVDAVKPQV AAENISKILY PEDSTPQGKA LRLEQQYFFV AASIQDAIRV
FYPGEENPDL TTFPSKICFQ LNDTHPVIGI PELMRVLIDE YGYDWDTAWS ITNKSFNYTC
HTLLPEALEV WPAKLIGELL PRHLEIINKI NEQFVAELGT KTSDSAKIDR MRIVTDGEDP
QVHMAYLATY GGSHVNGVAA LHSQLLKDVT LRDFSDVYGD KFTNVTNGVT PRRFIRIANP
RLSALITEGL GTDRWLSDLD MLEGLVPLAK DDEFVKKFAA VKQANKVAFS NYAKREYDFD
IDPNTMVNSM IKRLHEYKRQ SLKILSVISQ YADIKSGKVS ADDILPRTVV FGAKAAPGYK
MAKLTIQLIN NVARVVNNDP DVKGKLAVYY PWNYNIRLAQ HLIPATDLDE QISQAGKEAS
GTGNMKFALN GAMTVGTLDG ANVEIRERVG AENFFLFGMT VDEVEALYAK GYEPKYYYEA
DPRLKQAVDM VAGGTFSEGD KGLYEPLVTD WLNKDYFMTL ADFSAYMDIQ GEIETLYREP
LEWSRKALLN VANSGFFSSD RAIDDYLRDI WETGPLGE
//
