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
//