ID A0A1Y0FZS6_9GAMM Unreviewed; 838 AA.
AC A0A1Y0FZS6;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:ARU28930.1};
GN ORFNames=CBR65_16605 {ECO:0000313|EMBL:ARU28930.1};
OS Cellvibrio sp. PSBB006.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1987723 {ECO:0000313|EMBL:ARU28930.1, ECO:0000313|Proteomes:UP000196143};
RN [1] {ECO:0000313|EMBL:ARU28930.1, ECO:0000313|Proteomes:UP000196143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB006 {ECO:0000313|EMBL:ARU28930.1,
RC ECO:0000313|Proteomes:UP000196143};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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}.
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DR EMBL; CP021382; ARU28930.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0FZS6; -.
DR KEGG; cell:CBR65_16605; -.
DR OrthoDB; 7229284at2; -.
DR Proteomes; UP000196143; Chromosome.
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:UP000196143}.
FT DOMAIN 8..115
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 838 AA; 95850 MW; B681A489B3A64117 CRC64;
MSTFDRPLPA PLIILNELAG DLHWSWNHGG DELWRQINDE VWEHTHNPVS VLQLTSDAHL
EHLATDPQFL YQLDNLVSAR QRYLHEPAWY SKQYPDNPLR GIAYFSMEFG LCDALPLYAG
GLGILAGDHL KTASDLGVPL VGIGLLYQEG YFRQSLGSDG WQQETYLYND PGSLPLQPLK
AEDGSWLHID TGFLCRQVRF RVWQVKVGRV QLYLLDSNDP RNRPSDRGIT SKLYGGSTGL
RLVQEIALGI CGWRLIETLG LDIDVCHLNE GHAAFATLER ARAYAERHRT DFWHALRVTR
SGNIFTTHTP VEAGFDRYPI SLLRRYISEF TQHLGITMDS LIRLGRARPD DQSELFNMAY
LAVRTCGRSN GVSRLHGEVS RRIFQPLFPR WPEREVPVGF ITNGVHVPTW DSPEADALWT
DLFGQERWRR GLDALDTRRL SEPSDKQLWQ MASRGRARLV DYVRRKLAEQ FRHETAPDYC
ELDMSSALDP NILTLGFARR FAEYKRPDLL LHDPDRLARI LCNDRCPVQL VVAGKAHPAD
TTGKQALQAW HRFVQRSDVC HHVVLIEDYD IALAQHLVQG VDVWLNMPRR PWEASGTSGM
KVLVNGGLNL SSLDGWWAEA YTPEVGWALG DGQEHRPEDD WHDAEQLYQL LENEVIPEFY
RRDSDGISRP WVNRIRASME QLTLRFSSNR MLQEYLDQLY IPAAANVQQR QQNNGQLARE
LQQWHDHLSS HWHEVHVDEL TVVTDEQGAH LEVTVYLGSL QSNQVDVQVV ADATAHWPAL
RQTLTLRDPL EGATHAYRYT GPLPDQRPVD HFTARVIGAH HQALIPMENG LIAWQKRS
//
