ID A0A1G7A9M7_9ACTO Unreviewed; 788 AA.
AC A0A1G7A9M7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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=SAMN05421878_102138 {ECO:0000313|EMBL:SDE11594.1};
OS Actinobaculum suis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinobaculum.
OX NCBI_TaxID=1657 {ECO:0000313|EMBL:SDE11594.1, ECO:0000313|Proteomes:UP000182744};
RN [1] {ECO:0000313|Proteomes:UP000182744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20639 {ECO:0000313|Proteomes:UP000182744};
RA Varghese N.;
RL Submitted (OCT-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}.
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DR EMBL; FNAU01000002; SDE11594.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7A9M7; -.
DR Proteomes; UP000182744; 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:UP000182744};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 631
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 788 AA; 89637 MW; 7EAB31F6C7A6DF80 CRC64;
MSAKLTQPLG AFTQSVSGVS AAGSAPHDFW YGLSELVVSK LADNWEKTRE RYRQGPRASY
FSAEFLMGRA LLNNLVNLGL VEEASAALAE YGLNLTDVLD EEPDAALGNG GLGRLAACFL
DSTATLNLPV TGYGILYRYG LFKQTFENGF QEEEPDAWME TGYPFVIRRE AEARLVSFAD
LTVNAVPYDM PITGYGTDNV NTLRLWKAEP LEEFDYDAFN SQRFTDAIVE RERVNDLCRV
LYPNDSTYEG KVLRVRQQYF FVSASLQELI ERYIETHGED LRGFGDYNTI QLNDTHPVLA
IPELMRLLLD DHGMSWEEAW AVVQKTFAYT NHTVLAEALE QWEVSIFQQV FPRIFEICEE
IDRRFRAELA EAGYDQGKIE YMAPIHGGRV HMAWIACYAS FSINGVAQIH SDILVRDTLH
DWHDIWPEKF NNKTNGVTPR RWLNNCNPQL AALLTEVLGD DSWVSDLDKL ATIEERGNEE
IYRRLLEIKR ANKEVFARWL YNRDGIEVPV DAMYDSMIKR LHEYKRQLLN ALYILDLYYR
LKDDPSLQVT PRVFIFGAKA APGYKRAKAI IKFINEVARL VNSDPQMQGR MKVVFVPNYN
VSPAEHIIPA TDVSEQISTA GKEASGTGNM KFMMNGALTL GTMDGATVEI VDAVGEENAY
IFGAREEELP ELKRTYDPRE KYETVPGLKR VLDSLVDGTL DDGGTGMFHD LLASLLDGSS
WEEADQYYVL GDFASYREVR DRMAADYQDE LEWARKCWIN ICRSGRFSSD RTISEYATDI
WKVSPEKI
//
