ID A0A0Q4NL99_9GAMM Unreviewed; 815 AA.
AC A0A0Q4NL99;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=ASF13_17350 {ECO:0000313|EMBL:KQN64024.1};
OS Erwinia sp. Leaf53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN64024.1, ECO:0000313|Proteomes:UP000050856};
RN [1] {ECO:0000313|EMBL:KQN64024.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN64024.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN64024.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN64024.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQN64024.1}.
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DR EMBL; LMLK01000002; KQN64024.1; -; Genomic_DNA.
DR RefSeq; WP_056232582.1; NZ_LMLK01000002.1.
DR AlphaFoldDB; A0A0Q4NL99; -.
DR STRING; 1736225.ASF13_17350; -.
DR Proteomes; UP000050856; 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:UP000050856};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 662
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 815 AA; 93111 MW; 3AC92C9AFE4653DF CRC64;
MNAPFSYASP TVSVDALKHS IAYKLMFTIG KDPSIANKHD WLNATLLAVR DRMVERWLRS
NRAQLSQDVR QVYYLSMEFL VGRTLSNALL AMGIYDDART ALEDMGFDLE ELIEEESDPG
LGNGGLGRLA ACFLDSLATL GLPGRGYGIR YDYGMFKQNI VEGRQAESPD YWLEYGNPWE
FQRFSTRYKV RFGGRIQHEG SRARWVETEE ILAMAYDQII PGFDTDATNT LRLWGAQASN
EINLGKFNQG DYFAAVEDKN HSENVSRVLY PDDSTYSGRE LRLRQEYFLV SATVQDILHR
HWVMHETFDN LADRIAIHLN DTHPVLAIPE LMRVLIDDAK FDWEDAFDVA CQVFSYTNHT
LMQEALETWP VDMIGKILPR HLQIIFDIND HFLKTIQDQY PNDWELLSRI SIIDENNGRR
IRMAWLAVVV SHKVNGVSEL HSNLMVQSLF ADFAKLFPNR FCNKTNGVTP RRWLALANPA
LSGVLDEAIG RNWRTDLSQL DDLKQHIDFP NFIEQVSEAK LVNKKRLAQF IAQKMDIVVD
PHAMFDVQIK RIHEYKRQLL NVLHVITRYN RIKADPQADW VPRVNIFAGK AASAYYMAKH
IIHLINDVAA VINSDPQVKN KLKVVFIPNY GVSLAQIIIP AADLSEQISL AGTEASGTSN
MKFALNGALT IGTLDGANVE MLEHVGEENI FIFGNTTPQV EALRAEGYNS HPYYEQDAEL
HLALTQIATG VFSPQEPGRY RNIFDSLVNL GDHYQLLADY RSYVDEQDKV DKLYRNQEEW
TRRAVHNIAN MGYFSSDRTI QEYADEIWGI KPVKL
//
