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Database: UniProt
Entry: A0A1M4VVI9_9CLOT
LinkDB: A0A1M4VVI9_9CLOT
Original site: A0A1M4VVI9_9CLOT 
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
//
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