ID A0A252BJQ6_9PROT Unreviewed; 835 AA.
AC A0A252BJQ6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:OUJ05496.1};
GN ORFNames=HK24_12405 {ECO:0000313|EMBL:OUJ05496.1};
OS Gluconobacter sp. DsW_058.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=1511210 {ECO:0000313|EMBL:OUJ05496.1, ECO:0000313|Proteomes:UP000194786};
RN [1] {ECO:0000313|Proteomes:UP000194786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Winans N.J., Newell P.D., Douglas A.E.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047}.
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:OUJ05496.1}.
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DR EMBL; JOPH01000068; OUJ05496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A252BJQ6; -.
DR Proteomes; UP000194786; Unassembled WGS sequence.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR InterPro; IPR011834; Agluc_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR NCBIfam; TIGR02094; more_P_ylases; 1.
DR PANTHER; PTHR42655; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR42655:SF1; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF11897; DUF3417; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000194786}.
FT DOMAIN 15..116
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 601
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 835 AA; 93493 MW; 1520F2BD3A435586 CRC64;
MVDTSPRKPR AAEAALRMLA LDLHWTWNHE ADLLWQTINP DLWSRTCNPW ITLTRTPKAQ
LWEALQNPDV RNLLKASMER RKYELERSTW FAEKYTDAGL SEVAYFSMEY MLSEALPIYS
GGLGNVAADQ LKAASDLGVP VVAVGLLYAQ GYFRQVITPA GEQRALYPFN DPDQLPIQPV
LTPDGDWFRL SVQTATGEIW LRAWKAVVGR TTLYLLDTND PSNPPAVRCI TTQLYGGDAE
LRLRQEMVLG IGGWRLLHAL GHRPDICHLN EGHAAFAALE RARCLSEEEG IPFAQAQVIA
RAGTVFTTHT AVPAGFDRFP PKLIESHLTF YAEDRLGMPI QDFLALGRLD PTNKDEFFNM
AYLAVRCSGA VNGVSQLHGA VSRSLFTPLF PRWPQNEVPI SHVTNGVHTP TWDSASADEL
WTQVGGRSRW EGDLEGLGDA VRHLDDDTLW RSRCNSRAEF VHALGQELSA RQCIVGEDGL
WCLPAPSLNP EALTIGFARR FATYKRPDLL LYDEERLVRL LRDAQRPVQI VLSGKAHPQD
LEGQAMITRW VQFCQRQDIV GKVVFLADYD MALAQKMVQG VDLWLNTPRR PWEASGTSGM
KVLVNGGLNL SELDGWWAEA YAPEVGWALG DGLEHAGDPA YDHSDAQELY RLLEEHVLPE
FYERDAGGTP CAWVAKMRES MARLTPQFSA NRTVRDYTEQ FYLTGAQRYR RRLSDHGVSA
GTVLDRQNAL SAGWNSLRIG EVIIPENGGE QKAHAFIHPG MLDPALLRVE LYADAQDGHP
RIKSLTQGEH LPDGWIAYTL ETELPAPVAE CTLRIIPAAE VMSVPLEAPF ILWQR
//
