ID A0A2T0RY02_9RHOB Unreviewed; 797 AA.
AC A0A2T0RY02;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-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=CLV78_101157 {ECO:0000313|EMBL:PRY26064.1};
OS Aliiruegeria haliotis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Aliiruegeria.
OX NCBI_TaxID=1280846 {ECO:0000313|EMBL:PRY26064.1, ECO:0000313|Proteomes:UP000239480};
RN [1] {ECO:0000313|EMBL:PRY26064.1, ECO:0000313|Proteomes:UP000239480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29328 {ECO:0000313|EMBL:PRY26064.1,
RC ECO:0000313|Proteomes:UP000239480};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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:PRY26064.1}.
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DR EMBL; PVTD01000001; PRY26064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0RY02; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000239480; 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:UP000239480};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 639
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 797 AA; 90312 MW; 5977639A755C69D0 CRC64;
MTASEMKNAI LHHLVYTLGK DAAHAKTYDW RMALSFAVRD QIVDRWFEAT RRTYAEHRKR
VYYLSLEFLI GRLLKDAVIN MRLEEAVQDA LDALKIDWHE LLEDEPDAAL GNGGLGRLAA
CFMESQATLG LPAMGYGIRY EHGLFRQSFE DGRQVEEPED WLSQTHAWEF VRPEVAIDIG
FGGHVQEIGS RANWYPSEML IAMAHDTPVI GWKGRWGNTL RLWESRPMHG FDLARFNRGD
YAAAAEPEAL ARTLSRVLYP DDHTEQGKEL RLKQEFFHTA ASIRDIIRRF ESEYDDLKLL
PKKAAIQIND THPAIAGPEL VRILHDERGM DFEEAVGIAR NTISYTNHTL LPEALETWGE
ARMGRLLPRH MQLIDRIDDL HRRETGTGHV NAHQDGKVHM GTLGFIMAHK VNGVAALHTE
LQKTTVFKDL HELHPDRIVN QTNGVTPRRW LLSCNPRLAS LITEGIGDGW VDHAEDLEKI
EPLVADPAWL DRYAAAKKAN KVDLSNWIAE TMEIGVDPDA IFDIQVKRIH EYKRQHLNLL
ETIAHWQEIR DNPNAGWVPR VKIFGGKAFP NYIYAKDMVR LANDMARVMN SDPLTSRYLK
VVFPPNYNVS LAERLIPAAD LSEQISTAGK EASGTGNMKL TLNGALTIGT LDGANVEIRE
LVGAENFFLF GMTAEEVMAR RAEAGHAARA IAEDHRLARA LEAIRSGIFS PDEPGRYHSI
TENLSHHDYF MVCSDFTDYW RAQREVDTAF TDPKDWARKA ALNTARAGWF SSDRTIRGYM
KDIWHTDAAP QVADAAE
//
