ID U1S2Y6_9ACTO Unreviewed; 809 AA.
AC U1S2Y6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=HMPREF1979_00870 {ECO:0000313|EMBL:ERH25007.1};
OS Actinomyces johnsonii F0542.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=1321818 {ECO:0000313|EMBL:ERH25007.1, ECO:0000313|Proteomes:UP000016536};
RN [1] {ECO:0000313|EMBL:ERH25007.1, ECO:0000313|Proteomes:UP000016536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0542 {ECO:0000313|EMBL:ERH25007.1,
RC ECO:0000313|Proteomes:UP000016536};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERH25007.1}.
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DR EMBL; AWSE01000042; ERH25007.1; -; Genomic_DNA.
DR AlphaFoldDB; U1S2Y6; -.
DR PATRIC; fig|1321818.3.peg.730; -.
DR HOGENOM; CLU_010198_1_1_11; -.
DR Proteomes; UP000016536; 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 652
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 809 AA; 91520 MW; 56BF438676C6130D CRC64;
MFQSAAKLLQ SATTMPDKGR RMTQKLVTSA PAQVRAVSGR PETAATLMEV WQGLSAAVVD
TIADDWYATE QKYSAGRQEH YFSAEFLMGR ALLNNLSNLG MVDEAREAVG SFGDSLSDVL
EQEPDAALGN GGLGRLAACF LDSCATLDLP VNGFGILYRY GLFKQLFEDG FQTEHPDPWM
EEGYPFVIRH EEAQRLVHYQ DMTVRAIPYD MPITGYGTKN VGTLRLWKAE PLEEFDYDAF
NSQRFTEAIV ERERTSDISR VLYPNDATYE GKVLRVRQQY FFCSASLQQI VENYVSHHGE
DLTGFADYNA IQLNDTHPVL AIPELMRILL DEHHLGWEEA WEVVTKTFAY TNHTVLAEAL
ETWEISIFDR LFPRITEIVR EIDRRFRMEM AERGLEQGTI DYMAPISGDK VRMAWIACYA
SYSINGVAAL HTEIIKRETL GEWHAIWPER FNNKTNGVTP RRWLRQCNPR LSALLDEVTG
SDTWVKDLTV LAEHTDSVDE SVYDRLAEIK HANKVDFAAW IAQREGIEID PEAIFDVQIK
RLHEYKRQLL NAIYILDLYF RMKQDPSLQV PKRVFIFGAK AAPGYIRAKG VIKLINAIAD
LVNNDPVVSK TIKVVFVHNY NVSPAEHIIP AADVSEQISM AGKEASGTSN MKFMMNGALT
LGTLDGANVE ILEAVGDDNA YIFGATEDEL PGLRESYDPV WHYENVPGLK RVLDALTDGT
LDDNGSGWFA DLRRSLLEPS CEPADVYYVL GDFASYRETK DAMAADYADT RAWQRRAWVN
ITRSGRFSSD RTISDYAREV WKIDPEPIA
//
