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Database: UniProt
Entry: D9SFQ5_GALCS
LinkDB: D9SFQ5_GALCS
Original site: D9SFQ5_GALCS 
ID   D9SFQ5_GALCS            Unreviewed;       824 AA.
AC   D9SFQ5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   OrderedLocusNames=Galf_1326 {ECO:0000313|EMBL:ADL55352.1};
OS   Gallionella capsiferriformans (strain ES-2) (Gallionella ferruginea
OS   capsiferriformans (strain ES-2)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Gallionella.
OX   NCBI_TaxID=395494 {ECO:0000313|EMBL:ADL55352.1, ECO:0000313|Proteomes:UP000001235};
RN   [1] {ECO:0000313|EMBL:ADL55352.1, ECO:0000313|Proteomes:UP000001235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES-2 {ECO:0000313|EMBL:ADL55352.1,
RC   ECO:0000313|Proteomes:UP000001235};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Davenport K.W., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., Shelobolina E.S., Picardal F., Roden E., Emerson D.,
RA   Woyke T.;
RT   "Complete sequence of Gallionella capsiferriformans ES-2.";
RL   Submitted (AUG-2010) 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}.
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DR   EMBL; CP002159; ADL55352.1; -; Genomic_DNA.
DR   RefSeq; WP_013293291.1; NC_014394.1.
DR   AlphaFoldDB; D9SFQ5; -.
DR   STRING; 395494.Galf_1326; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   KEGG; gca:Galf_1326; -.
DR   eggNOG; COG0058; Bacteria.
DR   HOGENOM; CLU_010198_1_1_4; -.
DR   OMA; WLKQANP; -.
DR   OrthoDB; 7229284at2; -.
DR   Proteomes; UP000001235; Chromosome.
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:UP000001235};
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;  93363 MW;  A45D66C4F682F1C9 CRC64;
     MSSSKKPNSA QLDRSNPEVL QRMLSNHLIY TEGKSVATAT ERDWFEASAH AVRDQMIEKH
     LKTTEACVDQ DPKRLYYLSL EFLIGRTLSN AALNMGLEPA LRDSLKALGH DLEEVEETEI
     DAALGNGGLG RLAACFLDSM ATLDLPGQGY GIRYEYGMFN QRIKNGQQVE RPDNWLRFGN
     PWEFQRPERM YPVKFFGRVV QFSDGDGGIE HHWVDSDTVM AMAYDVPIPG YNTGTVNNLR
     LWAAKAAREF NLESFNAGDY LSAVQDKNIS ESLSKVLYPN DSSAVGKELR LRQEYFFVSA
     SIQDILYHFL QKHSDWNQLP EKVAIQLNDT HPAVGVAELM YQLIDVHGLK WDHAWGLVTK
     IFAYTNHTLM PEALETWAVE KFERVLPRHL EIIYEINHRF LAQVNHLFPG DTELLSRVSI
     INESHGRRVR MAHLAVVGSH TVNGVAAIHS GLLQTTLFAD FHRIYPEKFI NVTNGITPRR
     WLNQCNHNLA QLISSRIGNG FVRNLDQLKG LIPHAEDAEF RKQFRAVKQE NKARLAEYIK
     EKVGITVDIN SMFDVQIKRI HEYKRQLLNV LHVITLYNRI RSGNAHTITP RTIIFAGKAA
     PGYKLAKMII RLINDVASIV NEDPAVHGLL KVVFLPNYDV SSAEKLFPAS DLSEQISTAG
     TEASGTGNMK MALNGALTIG TLDGANVEIL EEVGDNNIFI FGLTTPQVAD LRTKGYSAWD
     HYYGNEELRQ VLDMIGNGFF SVEEPDRYRQ IFDNLTHHGD HYLLLADYAS YISTQDKVSL
     LYQDKEEWTR RAILNVANMG KFSSDRTIME YADNVWNVKS LKQS
//
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