ID A0A2P7QMF9_9SPHN Unreviewed; 817 AA.
AC A0A2P7QMF9;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-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=C7I55_17425 {ECO:0000313|EMBL:PSJ39140.1};
OS Sphingomonas deserti.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2116704 {ECO:0000313|EMBL:PSJ39140.1, ECO:0000313|Proteomes:UP000241167};
RN [1] {ECO:0000313|EMBL:PSJ39140.1, ECO:0000313|Proteomes:UP000241167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GL-C-18 {ECO:0000313|EMBL:PSJ39140.1,
RC ECO:0000313|Proteomes:UP000241167};
RA Liu L., Li L., Liang L., Zhang X., Wang T.;
RT "The draft genome of Sphingosinicella sp. GL-C-18.";
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:PSJ39140.1}.
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DR EMBL; PXYI01000005; PSJ39140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7QMF9; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000241167; 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:UP000241167};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 666
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 817 AA; 90618 MW; DE25D62632F67327 CRC64;
MTASQLALPS QDEDVAALRR LIVNKLAYSV GKDPIAARAH DWFLATALAV RDRVIERWMT
STRATKAEKK KRVYYLSLEF LIGRSLVDSL HNLGLTETMR TALGELGVDL EALRGLEPDP
ALGNGGLGRL AACYMESMAS LAVPAHGYGI RYENGLFRQV IKDGEQQEFP DTWLEHRNPW
EFERPEVAYP IGFGGSVEAL AGNGGHAAIW RPAETVDAIA FDTPVVGWRG RHVNTLRLWS
ARAPDPLRLD TFNRGDHLGA LAARGRAEAI TQVLYPSDES EAGQELRLRQ EYFFASASIQ
DLLRRHLETA PLETLPDCVA IQLNDTHPAI GVAEMMRLLV DVHQVEWEKA WALTQGVFSY
TNHTLLPEAL ETWPVPLMER LLPRHMQIIY LINALHLDRL AEGGKTDPAL LATVSLIDEH
GPRRVRMGPL SFLGSHKVNG VSALHTELMK ETVFRDFHAL YPDRIVNKTN GITFRRWLHE
ANPGLTRLLV EVAGESVLDK AEGLEMLAAH SGDSALHERL ARVRRANKEV LGGIIEERTG
IRVDPDAMFD VQIKRIHEYK RQLLNILETV ALYAAMRAHP TSDWTPRVKI FAGKAAASYH
RAKLIIKLIN DVAAVVNADA TLRGRLKVAF LPNYNVSLAE RIIPASDLSE QISTAGMEAS
GTGNMKLALN GALTIGTLDG ANVEILERVG ADNIFIFGMT AAEVEARRAA GIDMAETIAA
SPMLAQALEE LRSGRFSPGE PDRYRSLVDD LTHRDYFLVS ADFDAYASAQ AEVAQRWRDP
AAWWRSALLN IGGVSWFSSD RAVREYAEDI WNVPLAR
//
