ID A0A1M4VVI9_9CLOT Unreviewed; 752 AA.
AC A0A1M4VVI9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=SAMN02745158_01351 {ECO:0000313|EMBL:SHE73006.1};
OS Lactonifactor longoviformis DSM 17459.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Lactonifactor.
OX NCBI_TaxID=1122155 {ECO:0000313|EMBL:SHE73006.1, ECO:0000313|Proteomes:UP000184245};
RN [1] {ECO:0000313|EMBL:SHE73006.1, ECO:0000313|Proteomes:UP000184245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17459 {ECO:0000313|EMBL:SHE73006.1,
RC ECO:0000313|Proteomes:UP000184245};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQVI01000005; SHE73006.1; -; Genomic_DNA.
DR RefSeq; WP_072850211.1; NZ_FQVI01000005.1.
DR AlphaFoldDB; A0A1M4VVI9; -.
DR STRING; 1122155.SAMN02745158_01351; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000184245; 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 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:UP000184245};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 603
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 752 AA; 86316 MW; 622B4F8CDA0C60A7 CRC64;
MEFLERFQGL LKKDIREAAM EEIYCALLES VKACAAEKVQ QGENGEKKVY YISAEFLIGK
LLSNNLINLG VYDEVKRYIE DAGISFGEIE EFEPEPSLGN GGLGRLAACF LDSIATLGLN
GDGIGLNYHL GLFRQVFRGN QQKEMPNPWI EKKSWLTDTG IGFQVPFKDF TLKSRLFDID
VIGYENGVNK LHLFDVDTVD DSIVGDGISF NKKDIARNLT LFLYPDDSDE DGELLRIYQQ
YFMVSNGAQY ILKDCEEKGY DLHRLYEHAV IQINDTHPSM VIPELIRLLT DKGIPVEEAV
EIVSRTCAYT NHTILAEALE KWPVSYLEEV VPHLMPIIRM LAEKAAHTYK DPQVQIIDGE
NRVHMARMDM HYGFSVNGVA ALHTEILKNV ELKAFYKIYP EKFNNKTNGI TFRRWLLHCN
PRLTEFLDTC IGTGYKKDAS ELERLLSLKG DRKVQNRLLE IKAENKKELK SYLAKTLGVQ
LDENSIYDIQ IKRLHEYKRQ QMNVLYVIYK YLEIKKGNLP ETPVSVIFGA KAAPAYTIAK
DIIHVILCLQ EIIDRDPQVS PYLKVVMVEN YNVSMAEKLI PACDISEQIS LASKEASGTG
NMKFMLNGAV TIGTEDGANV EIHELVGDEN IYIFGESSRQ VIGHYEKSDY RAADYYIEDP
LIRELLNFII SPEMMRAGDP YHLLRIHAEL IQKDWFMTLL DLRDYIETKE RIYRDYEDRE
AWAEKMLVNI AKAGYFSSDR TISEYNRDIW RL
//