ID R9PPZ6_AGAAL Unreviewed; 824 AA.
AC R9PPZ6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=AALB_3547 {ECO:0000313|EMBL:GAD03467.1};
OS Agarivorans albus MKT 106.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Agarivorans.
OX NCBI_TaxID=1331007 {ECO:0000313|EMBL:GAD03467.1, ECO:0000313|Proteomes:UP000014461};
RN [1] {ECO:0000313|EMBL:GAD03467.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yasuike M., Nakamura Y., Kai W., Fujiwara A., Fukui Y., Satomi M., Sano M.;
RT "Draft Genome Sequence of Agarivorans albus Strain MKT 106T, an Agarolytic
RT Marine Bacterium.";
RL Genome Announc. 1:e00367-13(2013).
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:GAD03467.1}.
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DR EMBL; BARX01000028; GAD03467.1; -; Genomic_DNA.
DR RefSeq; WP_016403234.1; NZ_BARX01000028.1.
DR AlphaFoldDB; R9PPZ6; -.
DR STRING; 1331007.AALB_3547; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000014461; 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:UP000014461};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 670
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 824 AA; 93609 MW; 130C1CC8A93C69BA CRC64;
MAAKKAKATN TVALSKDQFK DAIVKHLRST CGTDEARANN QAWWKATCAA VNELVFERLT
ETSKANAEKD SRAVHYLSLE FLMGRLTVNN MHNVGVFGAA RDALADLGKD VNDICDEEPD
MALGNGGLGR LAACFIDSLA TLNYPAVGYG IHYEHGLFRQ EIQGGRQIER PDSWREYGNP
WEICRPESIQ EVPLYGYVET VFGEDGKMRK VWHAGRQIKG VPWDIPVVGY EAKTVNVLRL
WESKAADFFD WDVFNAGGYI DSQSEKSQAE AVSKVLYPND ESEAGKELRL IQQYFFCACS
LKDIIRRYKR NHSDFSQFSK QAVIQLNDTH PTVAIPELMR ILIDEEGLVW DDAWAICKET
FAYTNHTLLP EALEKWAVYL FEKVLPRHLE IIYEINRRFL EDEVEAKWPG NDEMKRHLSI
IEEGETRMVR MAFLCVVTCF KTNGVAAMHS ELVKEDLFPE FYELWPERFV NVTNGVTPRR
WLLACNEQLA NMYNETVGTD WPLKLDELKG AAKFADDAKF QKNFMAIKRE KKVELADKIE
ELCGIKVSPD AMFNVLIKRL HEYKRQHLAL LHILALYRRL LENPDYDMGP QVFIFGSKAA
PGYKLAKDII YAINKVADKV NNDPRIKDKL KVVFMPNYRV TLAEKLFPAG DVSLQISTAG
YEASGTGNMK FALNGALTLG TMDGANVEIR EEVGDENIFI FGMDCDEVKA LKAAGYNPWD
YYYGNPELKA VLDWLETDFF TPGAPGELAS IKHSLLEGGD PYLVLADFES FTTQYTAVDV
AYRDQKKWAK MAIINSASVG KFNSDRSIED YVDRIWKLEK VMPN
//
