ID R9KQX0_9FIRM Unreviewed; 821 AA.
AC R9KQX0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=C810_02029 {ECO:0000313|EMBL:EOS45932.1};
OS Lachnospiraceae bacterium A2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=397290 {ECO:0000313|EMBL:EOS45932.1, ECO:0000313|Proteomes:UP000014150};
RN [1] {ECO:0000313|EMBL:EOS45932.1, ECO:0000313|Proteomes:UP000014150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2 {ECO:0000313|EMBL:EOS45932.1,
RC ECO:0000313|Proteomes:UP000014150};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium A2.";
RL Submitted (APR-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOS45932.1}.
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DR EMBL; ASSX01000009; EOS45932.1; -; Genomic_DNA.
DR AlphaFoldDB; R9KQX0; -.
DR STRING; 397290.C810_02029; -.
DR PATRIC; fig|397290.3.peg.2227; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_9; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000014150; Unassembled WGS sequence.
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:UP000014150};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 658
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 821 AA; 95369 MW; 4823974DF6F3FEB3 CRC64;
MQNKMFEKKR FIQEIKDNVK NLYRKTLEEA SQQEVYQAVS QAVKEVVIDQ WLATQQTFEK
EDPKMVYYMS MEFLMGRALG NNLINLTAYQ EVKEALEEIG FDLNVIEDQE PDPALGNGGL
GRLAACFLES LSTLGYPAYG CGIRYRYGLF RQKIENGFQM EEPDNWLKDG YPFEMRRPEH
TFQVRFGGYV RSESDGNGKT RFIHEGYQTV RAVPYDMPVV GYNNNMVNVL IAWDAEPEKY
FELDAFDKGD YKKAVEQENL ARNLVEVLYP NDNHIQGKEL RLKQQYFFVS ASVQRAIARF
KKYHDDLHKL PEKVAIQLND THPTVAVAEL MRILLDEENM GWDEAWEITN KTCAYTNHTI
MSEALEKWPI EIFSRLLPRI YQIIEEINRR FILDIEKKFP GDHYKVKKMA IIYDGQVKMA
HLAIAAGCSV NGVARLHTEI LKEQELHEFY LMFPDKFNNK TNGITQRRFL YHGNPLLAEW
VNKYIGNDWV TDLPHLSKLA VYADDAKAQQ EFMNIKYQNK LRLAAYIRKH NGINVDPRSI
FDVQVKRLHE YKRQLLNILH VMYLYNKIKE HPEMDFYPRT FIFGAKAAAG YRIAKLTIKL
INSVAEVINN DASINGKLKV VFIEDYKVST AEWIFAAADV SEQISTASKE ASGTGNMKFM
LNGAVTLGTM DGANVEIVEE VGEENAFIFG MSSQEVIDHE QKRDYDPMQI FNSDQDIRQV
LMQLINGMYS QNDSELFRPL YNSLLNTHDT QYADTYFILK DFRAYAQAQE QVEQAYRDEK
RWAKMAMLNT AHAGKFTSDR TIQQYVDDIW HLDKVKVELP E
//
