ID Q0F289_9PROT Unreviewed; 831 AA.
AC Q0F289;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=SPV1_01897 {ECO:0000313|EMBL:EAU55661.1};
OS Mariprofundus ferrooxydans PV-1.
OC Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC Mariprofundaceae; Mariprofundus.
OX NCBI_TaxID=314345 {ECO:0000313|EMBL:EAU55661.1, ECO:0000313|Proteomes:UP000005297};
RN [1] {ECO:0000313|EMBL:EAU55661.1, ECO:0000313|Proteomes:UP000005297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV-1 {ECO:0000313|EMBL:EAU55661.1,
RC ECO:0000313|Proteomes:UP000005297};
RA Emerson D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (SEP-2006) 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:EAU55661.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AATS01000002; EAU55661.1; -; Genomic_DNA.
DR RefSeq; WP_009850680.1; NZ_DS022295.1.
DR AlphaFoldDB; Q0F289; -.
DR STRING; 314344.AL013_01150; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_0; -.
DR InParanoid; Q0F289; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000005297; 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:UP000005297};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 676
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 831 AA; 94866 MW; D30FF46284FBE583 CRC64;
MSDDIVSHQQ EITDVPPLDK DAASLVKGIQ RHYLRTLGQH TESHANHYKY QALAYTIRDH
LMENWKDTKD AYLKKDGKRA YYMSLEFLMG RALGNAILNL GLDDNVADAM HQLGLSYEEK
VELERDAGLG NGGLGRLAAC FIDSCATLSL PVTGYGIRYE YGMFRQLIHN GYQVEEPDHW
LNYGNVWEIT RPEYTQRVHF GGRSERYHDD QGKVRMRWTD TQDVLAIPYD TPIPGYKNHT
VNTLRLWKSA ATDEFDLSEF NAGDYTEAVS AKNHAEDISM VLYPNDASEN GKELRLRQQY
FLASASIKDV LRQWTREHGE DFSTFADKNV FQLNDTHPTV SVAELMRLLM DEYRLEWDDA
WAITTKTMAY TNHTLLPEAL ERWPVHLFGR LLPRLLDIIY GINAQFLSKV AEKWPGDVER
QRRMSIIEEG DVQQVRMAYL AIIGSFSVNG VAQLHSDLLV EGLFKDFYDM WPEKFNNKTN
GVTQRRWMAW CNKPLSSLIN NTIGDAWITD LQQLRKLAPS IENAEFRKQW ADCKRENKVR
LAKLVKSTCG VDFAPDAMFD VQVKRIHEYK RQLLNVLHVI HLYDRIKRGD TENWTPRCVL
IGGKAAPGYY MAKQIIKLVS NVADVVNHDP AVGDKLKVVF FPNYRVSAME VICPAADLSE
QISTAGKEAS GTGNMKFMMN GALTIGTLDG ANIEIREEVG DENFFLFGLT AEEVEKSRGH
YDPNAIIASD EDFLRVMNLL ECGHFSQFEP GLFAGICGAI RSCNDPWLVA ADFRSYVDAQ
QRAAEAYRDQ ESWVKMSILN TAYSGKFSTD RTMEDYNREI WKLQSIRPAS A
//
