ID V5FEF2_9VIBR Unreviewed; 817 AA.
AC V5FEF2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=malP {ECO:0000313|EMBL:GAD90053.1};
GN ORFNames=VHA01S_032_00030 {ECO:0000313|EMBL:GAD90053.1};
OS Vibrio halioticoli NBRC 102217.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219072 {ECO:0000313|EMBL:GAD90053.1, ECO:0000313|Proteomes:UP000017800};
RN [1] {ECO:0000313|EMBL:GAD90053.1, ECO:0000313|Proteomes:UP000017800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102217 {ECO:0000313|EMBL:GAD90053.1,
RC ECO:0000313|Proteomes:UP000017800};
RA Ichikawa N., Kimura A., Ohji S., Hosoyama A., Fujita N.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAD90053.1, ECO:0000313|Proteomes:UP000017800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102217 {ECO:0000313|EMBL:GAD90053.1,
RC ECO:0000313|Proteomes:UP000017800};
RA Isaki S., Kimura A., Ohji S., Hosoyama A., Fujita N., Hashimoto M.,
RA Hosoyama Y., Yamazoe A.;
RT "Whole genome shotgun sequence of Vibrio halioticoli NBRC 102217.";
RL Submitted (NOV-2013) 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:GAD90053.1}.
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DR EMBL; BAUJ01000032; GAD90053.1; -; Genomic_DNA.
DR RefSeq; WP_023404406.1; NZ_BAUJ01000032.1.
DR AlphaFoldDB; V5FEF2; -.
DR eggNOG; COG0058; Bacteria.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000017800; 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; 92777 MW; C0BED2E6A5C65CA4 CRC64;
MKPAQQKKFD KKQFQANVKK HLTATYATTE ENASTRQWYL AMGQALAELT TLDLLQTETD
KKITDAKSVN YLSLEFLIGR LTGNNLISMG LYEQVTDAMG ELGFNLTDLL EEERDPSLGN
GGLGRLAACF MDSCAAQEFP TVGYGLHYEY GLFKQSFKEG AQQEAPDAWR GIEGYPWELV
RPEIAQEIGF YGHVEVVMEN GEEKRRWVPG MTVKAMPWDL PIVGYESNTV YPLRLWECQA
IAPFSLESFN NGDYFEAQHS LIDAGNITKV LYPNDNHEKG KTLRLMQQYF HSAASIRDIL
RRHEAAGHAL VDLPKYETVQ LNDTHPTIAI PELMRILVDE KGFGWEKAWS ISTKTFAYTN
HTLLPEALET WSESLIQRLL PRHMEIIYRI NHDFLMEVRA KWPGDVDKQR KLSIIQEGFH
RMVRMANLCV VGSYAVNGVA ALHSSLVKKD LFPEFDELYP TRLHNVTNGV TPRRWLKFCN
PGLSALITEK IGDQWPAHLE QLSDISAFAE DKAFQKQYMA VKKENKQRLA NWVKENMDIE
LDTNAIFDVQ IKRLHEYKRQ HLNMLHILSL YHRLLNEPDF DMAPRVVFFA AKAAPGYHLA
KEIIYAINKI AEKINNDTRI GNKLKVVFMP DYRVSLAEII IPASDVSEQI STAGKEASGT
GNMKMALNGA LTIGTMDGAN VEIREEVGDE NIYIFGLDVD GVNDIRARGY NPFDYYNADH
LLKASMDLLL GEEFTPGEPG KLRATFDSLL DGGDPYLCLA DFASYVKAHE EMGEQYKDQS
GWAKKAILNT ALVGKFSSDR SIRDYVNNIW KLEPVHR
//
