ID A0A8J7DV26_9CYAN Unreviewed; 824 AA.
AC A0A8J7DV26;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=IQ249_06505 {ECO:0000313|EMBL:MBE9115546.1};
OS Lusitaniella coriacea LEGE 07157.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Spirulinales;
OC Lusitaniellaceae; Lusitaniella.
OX NCBI_TaxID=945747 {ECO:0000313|EMBL:MBE9115546.1, ECO:0000313|Proteomes:UP000654482};
RN [1] {ECO:0000313|EMBL:MBE9115546.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LEGE 07157 {ECO:0000313|EMBL:MBE9115546.1};
RA Castelo-Branco R., Eusebio N., Adriana R., Vieira A.,
RA Brugerolle De Fraissinette N., Rezende De Castro R., Schneider M.P.,
RA Vasconcelos V., Leao P.N.;
RL Submitted (OCT-2020) 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:MBE9115546.1}.
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DR EMBL; JADEWZ010000007; MBE9115546.1; -; Genomic_DNA.
DR RefSeq; WP_194028681.1; NZ_JADEWZ010000007.1.
DR AlphaFoldDB; A0A8J7DV26; -.
DR Proteomes; UP000654482; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0005980; P:glycogen catabolic process; IEA:TreeGrafter.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR FunFam; 3.40.50.2000:FF:000002; Alpha-1,4 glucan phosphorylase; 1.
DR FunFam; 3.40.50.2000:FF:000005; Alpha-1,4 glucan 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, LIVER FORM; 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 Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
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:UP000654482};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 656
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 824 AA; 94800 MW; 3921C5D04D96585F CRC64;
MSVETLKRAF ADNLFYTQGK DTSWATRRDY YMALAYTVRD RLFHRFFKTR KRYFAKDVKV
VCYLSAEFLM GRHLGNNLIN LGIYDRVNEA VRESGLDLGK LIELEHDPGL GNGGLGRLAA
CFLDSLATLE VPAIGYGIRY EFGIFHQAIK DGWQVEVPDK WLRFGNPWEI CRREASVQVK
FGGHTETYHD QQGNPRVTWI HDRTVTAIPY DTPVPGYNTN TVNTLRLWRA LAGDDFDFQA
FNAGDYDGAV ASKMSSETIS KVLYPNDNTP QGRQLRLEQQ FFFASASLQD IIRNHLRLHK
NLDALYEGVA IQLNDTHPTV AIAELMRLLI DEHQYYWDKA WYITQKTFAY TNHTLLPEAL
ERWPVSLFES LLPRHLEIIY EINHRFLEDI KTWFPDDEDR LGRMSIIEEF PEKSIRMANL
ACIGSHAING VAALHTELLQ KHTLRDFAEL WPEKFFNKTN GVTPRRWILL SNPKLSELIT
EKIGDGWLSN LDQLKQLEPF VEDADFRRRW REVKHENKLQ LTQYIWKHNS LEVDPHSIFD
VQVKRLHEYK RQLLSALNII TLYNRIKENP NADVFPRTFI FGGKAAPGYY MAKLIIKLIN
AVAEVVNKDP EVHGRLKVAF LANFNVSLGQ KIYPAADLSE QISTAGKEAS GTGNMKFAMN
GALTIGTLDG ANIEIREEVG AENFFLFGLT AEEVQSTKVQ GYNPMDYYHG NAELKAVIDR
IDSGYFSHGN QELFKPIVDS LLHHDQYMLL ADYQAYIDCQ EKVVEAYKDQ ERWTKMSILN
AARMGKFSSD RTINEYVNEI WKAKPVKVES EEYDSNNAGL NVQP
//
