ID F9RBU9_VIBSN Unreviewed; 817 AA.
AC F9RBU9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=VIBRN418_06141 {ECO:0000313|EMBL:EGU34345.1};
OS Vibrio sp. (strain N418).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=701176 {ECO:0000313|EMBL:EGU34345.1, ECO:0000313|Proteomes:UP000003627};
RN [1] {ECO:0000313|EMBL:EGU34345.1, ECO:0000313|Proteomes:UP000003627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N418 {ECO:0000313|EMBL:EGU34345.1,
RC ECO:0000313|Proteomes:UP000003627};
RA Strain E.A., Brown E., Allard M.W.;
RL Submitted (AUG-2011) 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:EGU34345.1}.
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DR EMBL; AFWD01000045; EGU34345.1; -; Genomic_DNA.
DR RefSeq; WP_009733715.1; NZ_AFWD01000045.1.
DR AlphaFoldDB; F9RBU9; -.
DR eggNOG; COG0058; Bacteria.
DR Proteomes; UP000003627; 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:SF25; MALTODEXTRIN 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 664
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 817 AA; 92934 MW; 23C76BE9503BC96F CRC64;
MKPLQQTQFD KTSFQNSVKK HLSATYATTI EQASSRAWYL AMGRALAELT TFDLLETEQD
ERIRNAKSVN YLSLEFLIGR LTGNNLISMG LYEQITEAMN ELGQNLTDLL EEERDPSLGN
GGLGRLAACY MDSLAAQEYP TVGYGLHYEY GLFKQSFVEG HQQEAPDAWC GVEGYPWEIA
RPELAQEIGF YGHVEVYQDQ GRERRRWVPG MSVKAMPWDI PIVGYQSETV YPLRLWECRA
IAPFSLESFN NGNYFEAQHA LIDAGNITKV LYPNDNHEKG KTLRLMQQYF HSAASVRDIL
RRHEEAGHDL ASLPQYETIQ LNDTHPTIAI PELMRIFMDE KGLEWADAWA ICSKTFAYTN
HTLLPEALET WSESLIQRLL PRHMEIIYQI NHLFLQEVRA KWPGDVAKQQ KLSIIQEGFH
RMVRMANLCV VGAYAVNGVA ALHSQLVKRD LFPEFNELYP GRLQNVTNGI TPRRWLKFCN
PGLSQLISEK IGDEWPAKLD QLEAISQYAN DAEFQQQFMA VKKANKQRLA DWVKRNMDIE
LDTNAIFDVQ IKRLHEYKRQ HLNMLHILSL YHRLLNDADF DMAPRVVIFA AKAAPGYHLA
KQIIYALNMI AEKINNDPRI GNKLKVVFMP DYRVSLAEII IPAADVSEQI STAGKEASGT
GNMKMALNGA LTIGTMDGAN VEIREEVGDD NIYIFGLDID EVEQVRNGGY NPYDYYNADP
LLKASLDLLV GEEFTPGEPG KLRATFDSLL DGGDPYLVLA DFASYIQAHE DMDKQYRDQA
GWAKKAILNT ALVGKFSSDR SIRDYVNNIW QLQSVQR
//
