ID L0K9P5_HALHC Unreviewed; 849 AA.
AC L0K9P5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:AGB41094.1};
GN OrderedLocusNames=Halha_1145 {ECO:0000313|EMBL:AGB41094.1};
OS Halobacteroides halobius (strain ATCC 35273 / DSM 5150 / MD-1).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Halobacteroides.
OX NCBI_TaxID=748449 {ECO:0000313|EMBL:AGB41094.1, ECO:0000313|Proteomes:UP000010880};
RN [1] {ECO:0000313|Proteomes:UP000010880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35273 / DSM 5150 / MD-1
RC {ECO:0000313|Proteomes:UP000010880};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Gu W.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "The complete genome of Halobacteroides halobius DSM 5150.";
RL Submitted (FEB-2012) 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; CP003359; AGB41094.1; -; Genomic_DNA.
DR RefSeq; WP_015326819.1; NC_019978.1.
DR AlphaFoldDB; L0K9P5; -.
DR STRING; 748449.Halha_1145; -.
DR KEGG; hhl:Halha_1145; -.
DR PATRIC; fig|748449.3.peg.1104; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_9; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000010880; 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:UP000010880}.
FT DOMAIN 13..123
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 606
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 849 AA; 98326 MW; 82B9650D1E3794F2 CRC64;
MEFHGSFSVK SKLPNRIKKL KEVAYNLWWC WNHRAELLFS KIDDKLWKEF DRNPVKLLSK
VDQERLNKLA SDNQFLVEYD QVISEFNDYL TTDDTWFKDV SPQWSEDEVI AYFSTEFGFH
ESIPIYSGGL GVLAGDHCKS ASDLGLPLIG VGLLYHEGYF KQRITDKGWQ ESLYPTLDET
YLPITAVQDQ EGNDLKVSVK LANREVLIKI WRLNVGRIKV FLLDTNIAEN SSQDRELTSR
LYGGGEETRI SQEIILGIGG TKGLAALGYD PVVWHMNEGH SVYLGLERIE ELMTEESLSF
TEALEVVAAS SVFTTHTPVP AGNEVFPFEL KEKYFSEYWK RIGLTKEEFM NLGCVYDMEK
DDGFCLTVLA LRLARFNNGV SKLHGEVSSQ MWEDIWEGIP TDENPIDAIT NGIHTLTWLA
PAWEELLDQY LPSDWRKRIE DKKMWQQVRN IPNKEFWQVH NQLKSKLIDY VREKDLARRK
RYNTLAKLDN NLLDKDKLTI GFARRFATYK RATLIFADLD RLNKICNKTG KEVQFIFAGK
AHPADVPGQE LIKKIHEISQ SEEFKGKVII LEDYDMNLAR YLIQGVDIWL NNPRRPLEAS
GTSGQKVAAN AGLNFSVLDG WWCEGYNKKN GWAIGYEIEY DDQEKQDQID SNSLYQVLEE
EIVPLYYDNI SQGIANDWIA SMKEAMISNI SVYSTDRMVQ EYTKKLYLPA VKRKNEVEAN
EYALAKELVN WKEDLKENWE ELKIKVRNKE KKEVYKVEDN INFSIEVDLA SLELDDIDVE
LYIVAEKLEQ PQIFVMDLEE KVSDNIYKYS LTLELSQLVG SGDYKYTFRV IPQDELLTTK
HELGLIKWI
//
