ID A0A1G5QH26_9GAMM Unreviewed; 835 AA.
AC A0A1G5QH26;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=SAMN03097708_02097 {ECO:0000313|EMBL:SCZ61185.1};
OS Thiohalomonas denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiohalomonadales;
OC Thiohalomonadaceae; Thiohalomonas.
OX NCBI_TaxID=415747 {ECO:0000313|EMBL:SCZ61185.1, ECO:0000313|Proteomes:UP000199648};
RN [1] {ECO:0000313|EMBL:SCZ61185.1, ECO:0000313|Proteomes:UP000199648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLD2 {ECO:0000313|EMBL:SCZ61185.1,
RC ECO:0000313|Proteomes:UP000199648};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FMWD01000006; SCZ61185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5QH26; -.
DR STRING; 415747.SAMN03097708_02097; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000199648; 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:UP000199648};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 679
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 835 AA; 95401 MW; 62D03D80DDC0D86D CRC64;
MGSEVLNKSQ VVQERTELQP LPMDQEAIGN GFLHYFSHFL GRDKYSESDH YTFAALALTL
RDRLMERWRR TRYAYESSDC KRTYYLSLEF LIGRSLGNSL LNLGVEEPVR KALHELGLQL
EEILDAEHDA GLGNGGLGRL AACFMDSCAS LQLPVRGYGL RYEYGMFRQQ IENGFQLEEP
DHWLRDGNPW ELERPEYTQR VQFGGRSETY QDGTGQTRWR WVATKDVLAV PYDVPVPGYQ
NDTVNTLRLW GAAATDEFDL GEFNAGSYPE SVEQKNAAEN ITMVLYPNDA SECGKELRLK
QQFFLASASL KDVLRWWVKH NGGDFIRFAD QNCFQLNDTH PSVSVAELMR LLMDEHGLGW
DQAWDITRHT MAYTNHTLLP EALERWPVSL FGSLLPRHLE IVYEINARFL EEVSRRWPGD
NDRLRRMSII EEGHEPQVRM AYLAIVGSFS VNGVAELHSR LLQEGLFLDF HQLWPEKFNN
KTNGVTQRRW LAWCNPGLSG LITERIGDGW IADLDQLHQL QSHADDPAFR ERWRDVKRAN
KVRLAELVEK ECGVHFDPDA MFDVQVKRIH EYKRQLLNIL HVIHLYDRIK SGDTSEWTPR
CVLIGGKAAP GYFIAKLTIK LINNVANVIN SDPEVGNRLK VAFVPNYRVS AMEVICPGTD
LSEQISTAGK EASGTGNMKF MMNGAVTIGT LDGANIEIRE QVGDDNFFLF GLNAQEVRTT
REEYDPNTII AANRDLARVM QLLESGHFNR FEPGLFDPIV DSIRTPHDPW LVAADFTGFV
AAQEQAAAAY RDREHWTRIS ILNTAGSGRF STDRTMLDYN RDIWKLEQVK PLNGE
//
