ID U2PYJ1_9CLOT Unreviewed; 811 AA.
AC U2PYJ1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 13-SEP-2023, entry version 37.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=CINTURNW_3886 {ECO:0000313|EMBL:ERK28864.1};
OS Clostridium intestinale URNW.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1294142 {ECO:0000313|EMBL:ERK28864.1, ECO:0000313|Proteomes:UP000016721};
RN [1] {ECO:0000313|EMBL:ERK28864.1, ECO:0000313|Proteomes:UP000016721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URNW {ECO:0000313|EMBL:ERK28864.1,
RC ECO:0000313|Proteomes:UP000016721};
RX PubMed=24136853;
RA Lal S., Ramachandran U., Zhang X., Sparling R., Levin D.B.;
RT "Draft Genome Sequence of the Hydrogen- and Ethanol-Producing Bacterium
RT Clostridium intestinale Strain URNW.";
RL Genome Announc. 1:e00871-13(2013).
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:ERK28864.1}.
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DR EMBL; APJA01000025; ERK28864.1; -; Genomic_DNA.
DR RefSeq; WP_021803808.1; NZ_KI273145.1.
DR AlphaFoldDB; U2PYJ1; -.
DR STRING; 1294142.CINTURNW_3886; -.
DR PATRIC; fig|1294142.3.peg.4050; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_9; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000016721; 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:UP000016721};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 656
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 811 AA; 93915 MW; CDCABBF666CEC037 CRC64;
MLTISKDRFK RDYIQKFIEL HGKDLDEGTN LNKYEALGSL IRDYVSRMWI ETNKRYNREK
EKQVYYFSME FLLGRLLGNS LLNLGIRDVC KKALKELGVE LEDLENLEQD QGLGNGGLGR
LAACFLDSMA SLKIPGNGCG IRYKYGFFEQ KIIEGSQVES PDKWLREGNV WEIKKTDKAE
VVKFGGEIKT EYIGGRLTFT HVNYEPVLAV PHDTPIVGFE NEVINTLRLW SAEPVVNEFD
FSSFSRGEFL KAIEYKNSVE AISQVLYPDD SFYEGKILRL KQQYFFVSAG IQSIIRHYKK
HLGDLCLLNE KIAIHINDTH PTLAIPELMR ILLDEEGLSW EDAWRITTNS VSYTNHTILQ
EALEKWPIDM FKKLLPRIFM IVEEINERFT KELWSKYEGQ WDKISQMAIV GDGYVRMAHL
AIVGSHSVNG VAKLHTEILK NQQMSDFYYM YPRKFNNKTN GITHRRWLIK ANPKLTSLLN
ETIGESWIKH PTDMEKFERF KNDSFVKESL FKIKNENKQK LAKIIKDNQG IVVDTNSIFD
VQVKRIHAYK RQTLNALRIM DLYNKLLENP SLDIAPRTFI FAGKAAPAYY LAKKTIELIT
ALADKINNDP RVSDKMKIVF MENYRVSLAE DIVPATEVSE QISTTTKEAS GTSNMKFMMN
GAITIATLDG ANVEIRDEVG DDNIVIFGLT EREVLEYYRH GKYSAWDTRN GDERLIKITD
QLVNGFYHDE KDRFRIIYEN LLNYNDEFFV LKDFASYIEA QEKVDKLYKN KEKWQEMSCV
NIAHSGIFSS DRTIKEYATG IWGSGYLYKN L
//
