ID A0A2Y9AAS6_9RHOB Unreviewed; 795 AA.
AC A0A2Y9AAS6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=BCF38_102531 {ECO:0000313|EMBL:PWJ21281.1},
GN SAMN05421539_102531 {ECO:0000313|EMBL:SSA41691.1};
OS Jannaschia seohaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=475081 {ECO:0000313|EMBL:SSA41691.1, ECO:0000313|Proteomes:UP000251571};
RN [1] {ECO:0000313|EMBL:SSA41691.1, ECO:0000313|Proteomes:UP000251571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25227 {ECO:0000313|EMBL:SSA41691.1,
RC ECO:0000313|Proteomes:UP000251571};
RA Cai Z.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWJ21281.1, ECO:0000313|Proteomes:UP000245839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25227 {ECO:0000313|EMBL:PWJ21281.1,
RC ECO:0000313|Proteomes:UP000245839};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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}.
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DR EMBL; QGDJ01000002; PWJ21281.1; -; Genomic_DNA.
DR EMBL; UETC01000002; SSA41691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Y9AAS6; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000245839; Unassembled WGS sequence.
DR Proteomes; UP000251571; 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:UP000245839};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 645
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 795 AA; 88277 MW; 561D2F1208DCA63C CRC64;
MPKDTITPPT AEALAQDVLA HLQTTLAKRQ SSATDHDWRV ALSLAIRDRV VTPWLDSLQR
TSETGGKEVY YLSLEFLIGR LIEDVTINLG LEDVAREAMA QLGQDYTALA AQEPDAALGN
GGLGRLAACF MDSLSTLGIP AHGYGIRYEH GLFEQHFQKG VQVETAEAWL AEQHVWEFER
PEVAYRIGFG GHVDYDAEGR ATWHPAQEVI AQAYDTPTVG WQAKWVNTLR LWSAKPVVHF
DLAAFNRGDY IGASASEALA RTLSRVLYPD DTTEQGRELR LKQEYFFVAA SLRDLVRRHL
KEGRALSTLP DYAAIQLNDT HPALAGPELI RLLVDEHGME FETAVKTARA CLGYTNHTLL
PEALERWSEG LMKHVLPRHY AIICLLNMAS LDETGTAILD HGEVRMGELA FVMAHKVNGV
SALHTELVKE TLFADLHKAY PDRIVNQTNG VTPRRWLHSA NPALSALITE TIGEGWVADL
ERLRELEPHI GTAAFDARFA DAKRANKAKL SDWLRQVHGA SVDPDAMFDI QIKRIHEYKR
QLLNILETVA LWNDIRDNPN GDWTPRVKIF GGKAAPGYVM AKSIIRLIND VGATINADPV
TRDLLQVVYP ENYNVSMAER LIPACDLSEQ ISTAGKEASG TGNMKLSLNG ALTIGTLDGA
NVEIREHVGA ENFFLFGLTA EEVRQRRTKP GHARSAIEAS PRLKRVLGQI ANGLFTGGEA
RYGDILGMLW DSDYFLVTAD FDSYYATQRE IDAAYRDQSD WTRKAALQTA RMGWFSSDRT
ISGYAGNIWN AASLL
//
