ID A0A0Q0JE95_9GAMM Unreviewed; 865 AA.
AC A0A0Q0JE95;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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 Name=malP {ECO:0000313|EMBL:KPZ70735.1};
GN ORFNames=AN944_02172 {ECO:0000313|EMBL:KPZ70735.1};
OS Shewanella sp. P1-14-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=1723761 {ECO:0000313|EMBL:KPZ70735.1, ECO:0000313|Proteomes:UP000050414};
RN [1] {ECO:0000313|EMBL:KPZ70735.1, ECO:0000313|Proteomes:UP000050414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-14-1 {ECO:0000313|EMBL:KPZ70735.1,
RC ECO:0000313|Proteomes:UP000050414};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:KPZ70735.1}.
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DR EMBL; LKTL01000012; KPZ70735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q0JE95; -.
DR PATRIC; fig|1723761.3.peg.2220; -.
DR Proteomes; UP000050414; 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:UP000050414};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 716
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 865 AA; 97696 MW; 9B70306B3C7DE089 CRC64;
MTVTKGKSTT EKPSIKDKSS VKKPAKTAKS GKAKQVKPDE LDTNSAVNQS TLEVVGSNHD
CDPCETLAAT FKRQIHGSLC RDEHAINDMY SALASTVKNQ LLNQWRETRL KDNQYQQKQV
AYLSLEFLMG RSLGNALLSL DLTKETHEAL AEYAADLESL QEAELDAGLG NGGLGRLAAC
FLDSCASLDL SVVGYGIRYE YGMFKQKMVD GYQVEQPDRW LREGNPWEVR MANHAITVPF
FGHTETYVDP SGDRHYVWVD TQDVQAIPHD MPVPGFRNGR INTLRLWKAE ATDDFDLAEF
NDGDYTEAVA RKNLAEQITM VLYPNDASEN GKELRLRQQY FLSSASLQDI LQRYTAVYGA
DFSQFSQRNV MQLNDTHPSI AVPELMRLLM DSYGLGWDEA WQVTTESMAY TNHTLLPEAL
ERWPVRMLGN MLPRILDIIY EINARYLEHV AHHWPGDTHK LASMSIIEEG AHPHVRMAYL
AIVASFSVNG VAGLHTQLLK QGLFKDFYSL WPHKFNNKTN GVTPRRWLVH CNPRLTQLIN
RRLGESWLTD LTQLTALNAF TDDKTFVKQW QQVKYDNKVE LAKLVLDECE VAFDPNMMFD
VQVKRIHEYK RQLLNILHVI HLYQRILSGD TKDLQPRCVL IGGKAAPGYA MAKQIIKLAN
NVAHMVNSDP IVSPYLRFAF LPNYNVSAME KICPGTDLSE QISTAGKEAS GTGNMKFMMN
GAMTIGTFDG ANIEMLEEVG EENFFLFGLR ADEVSELKSH YNPHDFIQQS PALANVINML
KSGHFNLVEP GIFDSIIAAI EDPFDQWMIA ADFEAYKQAQ EKVSLAYADQ QGWTQMSIRN
TASSGRFSSD NTISAYRDDI WLAKQ
//
