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Database: UniProt
Entry: B8ILB4_METNO
LinkDB: B8ILB4_METNO
Original site: B8ILB4_METNO 
ID   B8ILB4_METNO            Unreviewed;       839 AA.
AC   B8ILB4;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   OrderedLocusNames=Mnod_5267 {ECO:0000313|EMBL:ACL60113.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL60113.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL60113.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL   Submitted (JAN-2009) 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; CP001349; ACL60113.1; -; Genomic_DNA.
DR   RefSeq; WP_015931723.1; NC_011894.1.
DR   AlphaFoldDB; B8ILB4; -.
DR   STRING; 460265.Mnod_5267; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   KEGG; mno:Mnod_5267; -.
DR   eggNOG; COG0058; Bacteria.
DR   HOGENOM; CLU_010198_1_1_5; -.
DR   OrthoDB; 7229284at2; -.
DR   Proteomes; UP000008207; 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:UP000008207};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   REGION          8..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         689
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   839 AA;  92473 MW;  0C4AD48D3930D732 CRC64;
     MLNEVLLAGD RRTDAAADEP RAGWRPPVPS LSPSADTVTL LHDAILRKLA YAIGKSPATA
     RDRDWFAATA LALRDRVLDA CLSSAAPPVP QKRVYYLSLE FLIGRLLSDV MGNLGLAETA
     RAALAQLGVD LDAVAGAEPD AALGNGGLGR LAACFMESMA SLAIPAYGYG IRYDHGLFRQ
     VIEDGIQREV PETWLAEGNP WEFERPDSAC MVGFGGEVAM TVLADGAIRR VWRPAELVRA
     VPFDTPVVGW GARHVNVLRL WQARALEPID LARFNAGDHV GAVAERSRVE AISRVLYPSD
     GTPAGQELRL RQEFFFTSAS LQDLVRRHIA ERGDLRTLPD HAAIQLNDTH PAIAVPELMR
     LLVDEHGLPW DDAWHVTTHT LGYTNHTLLP EALETWPVEL MERLLPRHMQ IIYLINWMHL
     EGLSKHGKVD AGQLAAVSLI DEAHGKRVRM GHLAFLGARR VNGVSALHTE LMRQTVFAPL
     HALDTDKIVN KTNGITFRRW FHNANPGLTR LSVEAVGARV LDDPTALEGL ARFAEDAAFQ
     ERYAAVRRER KEALARVVKD RTGIAIDPAA LFDVQIKRIH EYKRQLLNIL ETVALYQAIL
     AEPQRDWPAR VKLFAGKAAS SYHQAKLIIR LACDVAKRVN ADPVVAGRLQ VAFVPNYSVS
     LAEAIIPAAD LSEQISTAGL EASGTGNMKL ALNGALTIGT LDGANIEIRE HVGDENIFIF
     GLTAAGVQAT TAEPGYAARA IAASPRLKAA LDLIASGGFS PEEPHRFRPL VDELTGQDRY
     LLTADFDDYW RVQREVDAAW RRPRTWWRAA ILNTARTAWF SSDRTMREYA EDIWRVEVA
//
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