ID A0A498D255_9BACI Unreviewed; 809 AA.
AC A0A498D255;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 13-SEP-2023, 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=D8M04_17395 {ECO:0000313|EMBL:RLL41299.1};
OS Oceanobacillus piezotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=2448030 {ECO:0000313|EMBL:RLL41299.1, ECO:0000313|Proteomes:UP000270219};
RN [1] {ECO:0000313|EMBL:RLL41299.1, ECO:0000313|Proteomes:UP000270219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-02 {ECO:0000313|EMBL:RLL41299.1,
RC ECO:0000313|Proteomes:UP000270219};
RA Yu L.;
RT "Oceanobacillus sp. YLB-02 draft genome.";
RL Submitted (OCT-2018) 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:RLL41299.1}.
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DR EMBL; RCHR01000008; RLL41299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498D255; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000270219; 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:UP000270219};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 658
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 809 AA; 94094 MW; F33EC15098677708 CRC64;
MQQLTSERLK EKIVNRLIIE NGIDVNDATN KQIFYALSSV VNEEILPNWF NTNKHYEKTG
YKQVYYLSME FLIGRLLESN LLNCGMLASA KEAINELGFS PEEIFAEEHD AGLGNGGLGR
LAACFLDSLA SLRYPGHGYG IRYRYGLFEQ RIIHGNQVEL PDYWLKEPYP WEIRKEEEAV
VIQYHGKVHM FKRNDGTLEF KYENTDKVMA VPYDVPVVGY NNEVVNTLRL WSAEPAFQDD
ARSQGDQSAF YHDLDHHHSI EQISGFLYPD DSSYEGKELR LKQQYFLVSS SIQNIIKQFK
KTNKMPVSRL PEKVVIQIND THPSLAIPEM MRILMDEERM SWDSAWEVTT RTFAYTNHTT
LSEALETWPK DMIQNLMPRI YMIIDEINER FCKKIWFDYE ELRDKIPELA IIAYDRIHMA
RLAIVGSFSV NGVARIHTEI LKKKEMKDFY TLYPKKFNNK TNGITHRRWL LQANPHLAGL
ITDVIGPQWI NRPKQLIRLL KHSNDKALLE KFDEVKRNNK IALANYIHHQ TGILVDEKSI
FDVQIKRLHE YKRQLLNIFH VIYLYNELKD NPNQDLTPRT FIFAAKAAPS YYLAKEVIKL
INTVASIVNY DKEIQGKLKV IFLENYNVSL AEKIIPASDI SEQISTASKE ASGTGNMKMM
MNGALTLGTM DGANIEIHDL VGPENIFIFG LTADEVLDYY QNGGYNARDI YNKDDRVKRI
LDQLNQGEFG IHDIEFKDIY YNILFHNDSY FVLKDFEPYL ETHELVDRAY RDRLHWLNMS
VINIAHSGKF SSDQTIKEYA TDIWKINQV
//
