ID A0A147GZN8_9BURK Unreviewed; 822 AA.
AC A0A147GZN8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=NS331_09075 {ECO:0000313|EMBL:KTT22839.1};
OS Pseudacidovorax intermedius.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Pseudacidovorax.
OX NCBI_TaxID=433924 {ECO:0000313|EMBL:KTT22839.1, ECO:0000313|Proteomes:UP000072741};
RN [1] {ECO:0000313|EMBL:KTT22839.1, ECO:0000313|Proteomes:UP000072741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS331 {ECO:0000313|EMBL:KTT22839.1,
RC ECO:0000313|Proteomes:UP000072741};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:KTT22839.1}.
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DR EMBL; LDSL01000053; KTT22839.1; -; Genomic_DNA.
DR RefSeq; WP_058641684.1; NZ_LDSL01000053.1.
DR AlphaFoldDB; A0A147GZN8; -.
DR PATRIC; fig|433924.3.peg.3795; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000072741; 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:UP000072741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 665
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 822 AA; 92414 MW; 95ED9F7277DB661E CRC64;
MTPATFEYDH PDRDVAAFKR SVATKLMYAV GKDPFAASQD DWLHATALAV RDLLVERWMA
TTRASYAQDV KRVYYLSMEF LIGRTFTNAL LAVDLYDTVK AALADFDIDV AALGEREPDA
ALGNGGLGRL AACFLDSMAT LGVPGMGYGI RYEYGMFRQR IIDGQQVETP DYWLTRGNPW
EFQRPEVKYR VRFGGHVEGR QAYGAAKWVG THDVLAMAYD TIIPGYGTQA TNTLRLWSAR
ATEEIDLSAF NRGNYFEAVE SKNHSENVSR VLYPDDSTLS GKELRLHQEY FFCSASVQDL
VRRYLRTHEG FGQLHEKVSI HLNDTHPVLA VPELMRVLVD EYDVNWDEAW AQTQKVFSYT
NHTLMHEALE TWPVEMLGRV LPRHLQIIFD INARFLGEVA AQVGPDTDLM RRLSLVDESG
ERRVRMAYLA VLASHSVNGV SALHSELMTQ SIFADFARLF PERFNNKTNG VTPRRWLGQA
NPPLAALLDK RIGRGWRRDL AQLEALKPMA DQPTFVRAFR HAKRENKLRL ANWIEQHMGL
VVDTDAMFDV QVKRIHEYKR QLLNVLHVIT RYHRILDDPH GHHVPRVVVF AGKAASAYVT
AKQVIRLIND VAAVINADER VGKLLKVVFL PNYSVSLAEI IMPAADLSEQ ISTAGTEASG
TGNMKFALNG ALTIGTLDGA NVEMKDAVGD DNIFIFGNTT PQVAEIRAKG YQPRSFYEGD
AELRRVLDAI QSGAFSPGEP GRYQSLFDTL VNWGDHYLLL ADYAAYVAKQ AEVDALYRDP
EAWTRKAILN VAGMGVFSSD RTIAEYAHEI WRTRPVMLGK AG
//
