ID U2RBR3_9FUSO Unreviewed; 826 AA.
AC U2RBR3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=HMPREF1984_01895 {ECO:0000313|EMBL:ERK65954.1};
OS Leptotrichia sp. oral taxon 215 str. W9775.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=1321779 {ECO:0000313|EMBL:ERK65954.1, ECO:0000313|Proteomes:UP000016640};
RN [1] {ECO:0000313|EMBL:ERK65954.1, ECO:0000313|Proteomes:UP000016640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W9775 {ECO:0000313|EMBL:ERK65954.1,
RC ECO:0000313|Proteomes:UP000016640};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-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:ERK65954.1}.
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DR EMBL; AWVR01000075; ERK65954.1; -; Genomic_DNA.
DR AlphaFoldDB; U2RBR3; -.
DR STRING; 1321779.HMPREF1984_01895; -.
DR PATRIC; fig|1321779.3.peg.1792; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_0; -.
DR Proteomes; UP000016640; 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:UP000016640};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 662
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 826 AA; 95692 MW; 80E7792CD27BB31D CRC64;
MKGRSEMVLD KAELKNSILR KLRRQYGKTM EEAHEYEIYY AVSRATLDYV VEKWYNTKKT
YAKKHAKQIY YFSAEFLMGR YLGNNLINLQ MNEVIKETLT ELGIDINKVE DQEIDAGLGN
GGLGRLAACF LDSMATLKLP GHGYGLRYKY GMFEQRIENG FQVEYPDNWT KYGDPWSIKR
LDRVFEVKFG GKIEVHRDEV GKEYFKRVDT ENVLAVAYDV PIIGYGNDTV NTLRLWEARS
PEGFDLNLFN SQKYLMASEK AVEAEDISRV LYPNDTEKDG KMLRLKQQFF FTSASLQDIV
RRYKSIYGND FSKFHEKVAI QLNDTHPVVA IPELMRIFLD YEKLGWDEAW LICKKVFAYT
NHTILSEALE KWDISLFQPL LPRIYQIVEE INRRFMDELN ARYNGDWQKI QYMSIIGNGQ
IRMAWLAIVG SHKVNGVAAL HTEILKHSEL KDWYDLYPEK FLNKTNGITQ RRWLLKANPE
LAEMITELIG DKWITDLYEL KKLEQFIEND DVLNRLTEIK FNNKKKLAEY IKETTGIEVN
PNSIFDVQVK RLHEYKRQLL NILHIMDLYN KLKENPLLDI EPRTFIFGAK AAAGYRRAKG
IIKLINAVAE KVNNDTDIND KIKVVFLENY RVSLAEKIFP AADVSEQIST AGKEASGTGN
MKFMLNGAIT IGTLDGANVE IVEEAGSENE FIFGLKANEV EELQHSNSYN PFEEYNNVEG
LKKVIDQLGD GTYDDDHTGI FRELQASLLY GAEGSRPDVY FLLKDFDSYR DTQIELGKAY
RDRRNWAKKA LKNIANAGKF SSDRTIMEYA NEIWDVHPVE IENYID
//
