ID A0A3G8YMM0_9DEIO Unreviewed; 845 AA.
AC A0A3G8YMM0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Glycosyltransferase family 1 protein {ECO:0000313|EMBL:AZI42396.1};
GN ORFNames=EHF33_06220 {ECO:0000313|EMBL:AZI42396.1};
OS Deinococcus psychrotolerans.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=2489213 {ECO:0000313|EMBL:AZI42396.1, ECO:0000313|Proteomes:UP000276417};
RN [1] {ECO:0000313|EMBL:AZI42396.1, ECO:0000313|Proteomes:UP000276417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14-83T {ECO:0000313|EMBL:AZI42396.1,
RC ECO:0000313|Proteomes:UP000276417};
RA Tian J.;
RT "Deinococcus shelandsis sp. nov., isolated from South Shetland Islands soil
RT of Antarctica.";
RL Submitted (NOV-2018) 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; CP034183; AZI42396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G8YMM0; -.
DR KEGG; dph:EHF33_06220; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000276417; Chromosome 1.
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 Transferase {ECO:0000313|EMBL:AZI42396.1}.
FT DOMAIN 13..125
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 613
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 845 AA; 94590 MW; 30B415EE0B9B277D CRC64;
MNVIGKVTVL PRLPKALARL EELAYNLYWS WTPKAQALYQ TLDPANWERF QHNPVQTLLE
TPSARLESLA ADPDYLGNYH AVLADFDAYM NKGAWGKGEV WAATNAAELP PVAYFSMEYG
FHESLPIYSG GLGVLAGDHC KSASDLGLPF TAVGMLFHQG YFRQLFNKDG WQEEAYDELN
LTTLPIRPAL TKSGEVAKVS VRVAGRDVVM QVWSLRIGRI QVLLLDANVP ENSEDDRKMT
ARLYGGNQEL RIQQYVLLGV GGIRALRALD VPASVYHMNE GHAALMGLER MREYVAQGLD
FRTALEATAS STLFTTHTPV AAGNDAFAYE MMDRYIGDWP AQLATSRSEL YDLAEHAQNW
DGHLVPTFSM TVFALRMSRM ANGVSELHGE VSRGMWNFLY EGADEEEVPI GHVTNGAHNL
TFLAQQFRDL YSTVLPGNWI ERLEDKQMWD DINTIPDAQL SATQHELKEE MIAFVRVRLQ
EQLRRTGAPA AEVAAAGETL SADALTIGFA RRFATYKRAT LLFRDRERLS KIVNNPERPV
QFIFAGKAHP ADNPGKAFIQ EIYKLSRDPE FAGKIIIVEN YDMNVARHLV QGVDIWLNNP
RRPLEASGTS GMKASFNGAP NFSILDGWWR EGYDTTNGWP IGEEREYTDL NIQDDADSFS
MYETLENTIV PLYYGKDAQG QNHGWLKTVR RAIITVNPEF AMQRQVIDYV QQFYLPLAQR
AAKVDANNFE KARTLGSWKS WVRQQWQHVQ IHATAQLPAT VQPGEEVKVS AQVTPAGIQE
SELHVEAVLK HGEDTLHVPM KATGGGNYEV SIPLTDSGLY SVGVRAMPYS ADLSNPIELG
LIKWA
//