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Database: UniProt
Entry: Q3STC5_NITWN
LinkDB: Q3STC5_NITWN
Original site: Q3STC5_NITWN 
ID   Q3STC5_NITWN            Unreviewed;       831 AA.
AC   Q3STC5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 109.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   OrderedLocusNames=Nwi_1204 {ECO:0000313|EMBL:ABA04466.1};
OS   Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS   NCIMB 11846 / Nb-255).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Nitrobacter.
OX   NCBI_TaxID=323098 {ECO:0000313|EMBL:ABA04466.1, ECO:0000313|Proteomes:UP000002531};
RN   [1] {ECO:0000313|EMBL:ABA04466.1, ECO:0000313|Proteomes:UP000002531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255
RC   {ECO:0000313|Proteomes:UP000002531};
RX   PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006;
RA   Starkenburg S.R., Chain P.S., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA   Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA   Hickey W.J.;
RT   "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT   Nitrobacter winogradskyi Nb-255.";
RL   Appl. Environ. Microbiol. 72:2050-2063(2006).
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; CP000115; ABA04466.1; -; Genomic_DNA.
DR   RefSeq; WP_011314495.1; NC_007406.1.
DR   AlphaFoldDB; Q3STC5; -.
DR   STRING; 323098.Nwi_1204; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   KEGG; nwi:Nwi_1204; -.
DR   eggNOG; COG0058; Bacteria.
DR   HOGENOM; CLU_010198_1_1_5; -.
DR   OMA; WLKQANP; -.
DR   OrthoDB; 7229284at2; -.
DR   Proteomes; UP000002531; 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:UP000002531};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         682
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   831 AA;  93889 MW;  00CC9911097B3C88 CRC64;
     MAFDVPPKRL RSLDEDTPAW LEPEDDDIVA EIKSTILSKI VLVAGKDVKH ADIHDWYIAA
     ALTLRDRIVY QWLQSDRATQ NHGAKRAYYL SLEFLIGRLL TDALTNMSLM KPFRMAIEDL
     GLDFDELRNV EPDAALGNGG LGRLAACFME SMASLAIPAR GYGIRYEHGL FRQIISNGWQ
     EEFPEQWLLS GNPWEFERRD VVFDIQYSGR LDHAEEDDSE GRTLWIPDET IQAIAYDTPI
     VGWRGHHVNA LRLWSARAVD PMRLDTFNSG DHLGAMSEMA RAQAISKFLY PSDETPAGRE
     LRLRQEYFFV SASLQDILNR HLHTDGDIRS LPSHAAIQLN DTHPSLAVPE LIRLLMDRYH
     IGWNDALDIT TKTISYTNHT LLPEALETWP VELFERMLPR HLDIIYRINA EHLAAAEKHF
     GADARSQASV SLIDETGGRR VRMGHLAFVG SHRINGVSAM HSELMRETVF ADLNSLYPDR
     ITNKTNGITF RRWLHQCNPE LTSLLQDACG AAVLDEPERL RMLERLSDDP AFQQRFQTVK
     RTNKVALAQI IARQFGIVVD PSALFDVQIK RIHEYKRQLL NAIETIALYQ AILDDPQGNW
     TPRVKIFAGK AAASYRQAKL IIKLINDIGN VINNDPRIRD LLKVVFIPNY NVSAAEVIVP
     ASDLSEQIST AGMEASGTGN MKLALNGAIT IGTFDGANIE IAEHVGEENI HIFGMRADEV
     VQRRSMGLDA TDIITSSPKL ARVIEAIERG AFSPDDASRF IPIAHALRFL DHYLVSADFD
     DYYRAQRAVD TKWASPEWTH SSILNVARMA WFSSDRTIRE YAEDIWGIPV I
//
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