ID A0A2M8RT81_9PAST Unreviewed; 790 AA.
AC A0A2M8RT81;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=CVP04_11105 {ECO:0000313|EMBL:PJG82069.1};
OS Caviibacterium pharyngocola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Caviibacterium.
OX NCBI_TaxID=28159 {ECO:0000313|EMBL:PJG82069.1, ECO:0000313|Proteomes:UP000230282};
RN [1] {ECO:0000313|EMBL:PJG82069.1, ECO:0000313|Proteomes:UP000230282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7_3 {ECO:0000313|EMBL:PJG82069.1,
RC ECO:0000313|Proteomes:UP000230282};
RA Christensen H.;
RT "Reclassification of Bisgaard taxon 5 as Caviibacterium pharyngocola gen.
RT nov., sp. nov.";
RL Submitted (NOV-2017) 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:PJG82069.1}.
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DR EMBL; PHGZ01000031; PJG82069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8RT81; -.
DR Proteomes; UP000230282; 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:SF25; MALTODEXTRIN 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:UP000230282};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 642
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 790 AA; 90497 MW; B774EDF24F6B75E0 CRC64;
MALFHKNVQK YCRYFDVESP EQFSLEQWYQ IVAESTLDLV YSKPAVKGSE DRHVNYLSME
FLIGRLTGNN LMNLGCYEQI KTYLSQYNVE LVDVLEQERD PALGNGGLGR LAACFLDSMA
ALGQNATGYG LHYQYGLFKQ SFEQGEQKES ADTWNRDQYP WHSYNVSKTQ NVNFGGKIKL
VKGDKYEWKP ALTIQGKAFD LPIVGYQNDI IQPLRLWQAD SDQSFDLAKF NDGKFLNADK
TIVNATALTQ VLYPNDNHKA GQKLRLMQQY FHCACSVADI LERHFSEGYE LSDFASRQVI
QLNDTHPTLA IPELMRVLLD KYELTWDEAW SICSNTFAYT NHTLLPEALE QWDQRLFKQL
LPRHYQIVEK INNIFHDRVI AEFGEDNKVW EKLAILFDYR VRMANLCVVT CFAVNGVAQI
HSDLLVTDLF PEYHKLFPTK FCNVTNGITP RRWIRQANPQ LSDLLDRTVK ADWTKDLELL
RGVEDYVDDA GFREEYRRIK QVNKSVLADE IERTLGFAVN QDAIFDVQIK RFHEYKRQHL
NLLNIIATYQ SLKENPNQDY TPRLFVFAGK AAPGYYLAKN IIHAINNVAD LINNDKQVKD
KLQVAFLPDY RVSLAEKIIP AADVSEQISM AGKEASGTGN MKLALNGALT LGTLDGANVE
IAEMVGEENI FLFGHTVESV RELLAKGYQP KDYYKKDAVL KSAVDFLAKG KASNGDKAAF
NLMLDSLLER DPFLVFADFD SYRKAQDRIG QAYLDQEAWL RSAILNTARL GTFSSDRSIR
DYQSRIWLKK
//
