ID C9KN21_9FIRM Unreviewed; 825 AA.
AC C9KN21;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=glgP {ECO:0000313|EMBL:EEX68760.1};
GN ORFNames=MITSMUL_04832 {ECO:0000313|EMBL:EEX68760.1};
OS Mitsuokella multacida DSM 20544.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Mitsuokella.
OX NCBI_TaxID=500635 {ECO:0000313|EMBL:EEX68760.1, ECO:0000313|Proteomes:UP000003671};
RN [1] {ECO:0000313|EMBL:EEX68760.1, ECO:0000313|Proteomes:UP000003671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20544 {ECO:0000313|EMBL:EEX68760.1,
RC ECO:0000313|Proteomes:UP000003671};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-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}.
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:EEX68760.1}.
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DR EMBL; ABWK02000017; EEX68760.1; -; Genomic_DNA.
DR AlphaFoldDB; C9KN21; -.
DR STRING; 500635.MITSMUL_04832; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR PATRIC; fig|500635.8.peg.1525; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_9; -.
DR Proteomes; UP000003671; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 674
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 825 AA; 95309 MW; 42CE2E622A05EFE7 CRC64;
MFFLARETKE QKQKSREFDK LKENLKIRFV NTAHLMYGRE IKDLTKNEVY QTVAATAKQF
ISDNWIKTNK TYAERQEKQI YYFSIEFLLG RLLKSNLINL GIEEAVKEVL EDFDLSLVKT
FEEEPDAGLG NGGLGRLAAC FIDSMAAHRL PGHGCSIRYQ YGLFEQKIIE GNQVEIPDNW
LKNGFAWEYR KPDKAIDVKF NGNAYMKKMP DGSLKLVYEN PMTVMAVPYD VPIVGYHNNT
VNTLRLWNAE VNRDFSDYGR LTQEQMRQKN DYRNFVESIT RYLYPDDSTY DGRRLRLIQE
YFFVSAGVQS IVRHYKKVGM DIHDFAQKIA IHINDTHPAL CVAELMRILV DEEGLEWNEA
WAITKNTIAY TNHTIMPEAL EKWPIDMFKP LLPRIYMIID EINRRWLIDV RDRYPNNEQK
VHELSIIQDG MVHMARLSIV GSHSVNGVAK IHTDILKSTT LHEFYEYNPR MFNNKTNGIT
HRRWLMGANP ELSDLIDATI GSRRWHRHPE QLDLLNDYVE DKPFLEKLGA IKHLRKEALA
KYVKEHNGID VDPDSIFDIQ VKRIHSYKRQ LMNILHIMYQ YHKLKTDPNF DMLPTTYFFG
GKAAPGYYIA KETIRLINAV ADKINNDASI KGKIKVVFIE NFGVSIGEIV YPAADVSEQI
STASKEASGT GNMKFMMNGA ITLGTLDGAN VEIRDAVGGD ENCVIFGLKA EEVLNYYATG
TYSAWDEYNT NENVRLVVDQ LTDGTYGNFQ SLLDYLIRAN DEFFILKDFN AYADAHVEIM
KRYQKRFQWL KASAVNIANS GVFSSDRTID EYANEIWQVK PVMIP
//
