ID A0A2K0X273_9BIFI Unreviewed; 827 AA.
AC A0A2K0X273;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=BFS08_04445 {ECO:0000313|EMBL:PNP88605.1};
OS Gardnerella sp. KA00735.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=1973156 {ECO:0000313|EMBL:PNP88605.1, ECO:0000313|Proteomes:UP000236541};
RN [1] {ECO:0000313|Proteomes:UP000236541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00735 {ECO:0000313|Proteomes:UP000236541};
RA Bumgarner R.E., Fredricks D.N., Srinivasan S.;
RL Submitted (NOV-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:PNP88605.1}.
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DR EMBL; NBMV01000002; PNP88605.1; -; Genomic_DNA.
DR RefSeq; WP_075523630.1; NZ_NBMV01000002.1.
DR AlphaFoldDB; A0A2K0X273; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000236541; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 670
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 827 AA; 92782 MW; 02F0DF9955F9FC29 CRC64;
MTKHVAPKAK TTATAFAKEI QEHLKYTQGV TPEQATTADV YVAASVAVRR HLMDSWMQTQ
HDMVNGNTKA VGYLSAEFLM GKQLENALLN AGLTDQFNKA VTKLGFDPKA VIDAEYEPGL
GNGGLGRLAA CFIDSLASIG VPAFGYGIQY RYGIFKQRFD EEGKQVETPD YWLNNEEPWG
HIDYGRDQRV NFGGEVVEEN GKRVWKPAWS VRAVPVDYMV PGYNSGRVNT LRLWTAKSYD
EFDLLTFNKS DYLDAVKPQV AAENISKILY PEDSTPEGKA LRLEQQYFFV AASIHDAIRV
FYPGQDKPDL TTFPSKINFQ LNDTHPVIGI PELMRVLMDE YDYDWNTAWG ITTKTFNYTC
HTLLPEALEV WPAKLIGELL PRHLEIIQGI SEQFRNELRG KGVAEDQVER MRIATDADEN
GEGAVVRMAY LATYGGSYVN GVAELHSELL KDVTLKDFSS VYPDKFKNVT NGVTPRRFVR
LSNPRMSALI TEGLGTDAWQ GDLELLEGLK PLADDKAFVK KFAEVKKQNK LAFVDFAKQK
YGFEINPDTM FNTIIKRLHE YKRQSMKILQ VISMYAGIKN GTIDVDKMLP RTVFFGAKSA
PGYAMAKLTI QLINNVARVV NNDPACKGKL AVFFPPNYNI ELAMNLIPAT DLDEQISQAG
KEASGTGNMK FALNGALTVG TLDGANVEIR ERVGAENFFL FGMTVEEVDK LYAEGYDHGG
SRKYYESDPR LKTAVDMVAD GTFSNGDKSV YEPLVNDWLT HDYFMAMADF SSYMDIQAQI
EETYRDPMKW ARMAVLNVAN SGYFSSDRSI EDYLDRIWHT GALPTAE
//
