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
//