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
//