ID A0A370U657_9GAMM Unreviewed; 825 AA.
AC A0A370U657;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=DN730_14815 {ECO:0000313|EMBL:RDL43248.1};
OS Marinomonas piezotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=2213058 {ECO:0000313|EMBL:RDL43248.1, ECO:0000313|Proteomes:UP000254326};
RN [1] {ECO:0000313|EMBL:RDL43248.1, ECO:0000313|Proteomes:UP000254326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-05 {ECO:0000313|EMBL:RDL43248.1,
RC ECO:0000313|Proteomes:UP000254326};
RA Yu L., Tang X.;
RT "Marinomonas sp. YLB-05 draft genome sequence.";
RL Submitted (JUN-2018) 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:RDL43248.1}.
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DR EMBL; QKRA01000008; RDL43248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370U657; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000254326; 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 Reference proteome {ECO:0000313|Proteomes:UP000254326};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 671
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 825 AA; 94440 MW; 6C02B0858441DBB1 CRC64;
MTQSNQELLA SDTASYHGLK EGILYHLRYT LALRPEQATK RDWWLCLSMA VKDRIVDDMV
DTQDRHNQDN VRRLYYLSME YLMGRMLVNN VHNVGVFNEA QRALESLGLE WDEICDVEVD
MGLGNGGLGR LAACFLDSLA TMDFPAIGYG IYYEFGLFKQ EFQYGKQIEH PDTWINYGTP
WEIVRSEYAQ PVQYYGRVED SYDSFGNYHP RWVDTKSVLG IPHDIPVAGY DTKTVNFLRL
WSSRSTEDFD LDEFNNGDYV EAVRSKAIGE TISKVLYPND KTENGKELRL VQQYFFVACS
LADILRRFER SNGSNWDALP DKAAVQLNDT HPTIAIVELM RILVDDKRLH WDHAWGLVTR
IFAYTNHTLL PEALEKWSVA LLNKVLPRHL QLIFEINHRF MVQVEAQWPD RDDIKADMSI
IEEGPHRSVR MAHLAVVGSH TVNGVAALHS QLLKSDLFPR FHALYPNKFT NKTNGITPRR
WLLNCNPELT ALFEQYGIES DWPKNLERLR KLESLADDPV FQEAFMAVKH QKKQALARVI
FDECGIEVDS TALFDVQIKR LHEYKRQHLT LLNILTIYHR LLNNPDLDIV PRVFIFGAKA
APGYALAKTI IHAINAVADV VNNDGRIQGK LKVVFLPNYR VSLAAKIIPA ADLSEQISTA
GKEASGTGNM KLALNGALTI GTLDGANVEI REEVGEENIF IFGLSIEEVQ ALDRHGYNPH
QYYQQDEELR NAIDWLCSGY FSPNEPHAFD DIRAALLEHG DQFKAMADYR TYMECQQKVD
AVYRDPSRWA RMAILNTARM AKFSSDRTIQ EYAREIWNLP ACSVS
//
