ID   F0JK39_9BACT            Unreviewed;      1412 AA.
AC   F0JK39;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:EGB16288.1};
GN   ORFNames=DND132_3085 {ECO:0000313|EMBL:EGB16288.1};
OS   Pseudodesulfovibrio mercurii.
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae.
OX   NCBI_TaxID=641491 {ECO:0000313|EMBL:EGB16288.1, ECO:0000313|Proteomes:UP000007845};
RN   [1] {ECO:0000313|EMBL:EGB16288.1, ECO:0000313|Proteomes:UP000007845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND132 {ECO:0000313|EMBL:EGB16288.1,
RC   ECO:0000313|Proteomes:UP000007845};
RX   PubMed=21357488; DOI=10.1128/JB.00170-11;
RA   Brown S.D., Gilmour C.C., Kucken A.M., Wall J.D., Elias D.A., Brandt C.C.,
RA   Podar M., Chertkov O., Held B., Bruce D.C., Detter J.C., Tapia R.,
RA   Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Woyke T., Mikhailova N.,
RA   Ivanova N.N., Han J., Lucas S., Lapidus A.L., Land M.L., Hauser L.J.,
RA   Palumbo A.V.;
RT   "Genome sequence of the mercury-methylating strain Desulfovibrio
RT   desulfuricans ND132.";
RL   J. Bacteriol. 193:2078-2079(2011).
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; CP003220; EGB16288.1; -; Genomic_DNA.
DR   RefSeq; WP_014323712.1; NC_016803.1.
DR   SMR; F0JK39; -.
DR   STRING; 641491.DND132_3085; -.
DR   KEGG; ddn:DND132_3085; -.
DR   eggNOG; COG0058; Bacteria.
DR   eggNOG; COG0438; Bacteria.
DR   HOGENOM; CLU_005051_0_0_7; -.
DR   OrthoDB; 7229284at2; -.
DR   Proteomes; UP000007845; Chromosome.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 4.
DR   InterPro; IPR011834; Agluc_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR   InterPro; IPR008631; Glycogen_synth.
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; PF05693; Glycogen_syn; 2.
DR   Pfam; PF00343; Phosphorylase; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          579..685
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
SQ   SEQUENCE   1412 AA;  158954 MW;  A48299D5AAC1191C CRC64;
     MDKSWLFEVS WEVCNKVGGI YTVISSKAPQ AKAAFDNRYV AVGPLLDRNP GFLPSDPPDT
     VRPALERLKA WGIETATGQW DIPGKPLVLL IGFRNAFPAH DKLLFQLWND YGVDSMAGGW
     DYIEPVLFST AAAMAIKEIS EDVGEGADVY AHFHEWMSGA GVLHLKKHAP SVSTVLTTHA
     TMLGRAMSGA GVDIYKRLEE IEPSQEAKAY GVTAKHSMES VSAREADCFT TVSNITRREA
     SNLLGTNPAV VTVNGFNLDG FADPTAVAQT RKRSRKQLLD LAANFLERDL DPAKTLLVAT
     SGRYEFHNKG IDLLLDGLGD LNEELAKSGK DVTVVAFLLV SCGYAGFSDE ARRRLKQERY
     DIEKYAGIST HHLGDADHDP VVMKCRERKL DNEAVNRCCV IFIPVYLDGN DGVLNLEYYD
     ALAGMDLTVF PSFYEPWGYT PMESAAFAVP TVTSDRAGFG QWIMERHPQG HPGVHVLNRL
     EDDYETAREN LALYLSDFTR WTPEERVSRS KEARKIAEEA TWAHFYPRYL EAYEYAADIR
     TERIAGVQRM VAAPGAEISF SGVNTTQPRL RSFTVVTELP APLARLRDVA ENLWWVWHRD
     SQELFEWMDA DKWHESGHNP VLFLDTMRRD RLAELADDPE FIGRLNSVLE RFDAYMAESA
     KADVRGITWK NPVAYFSMEF GLHEAIPVYS GGLGLLSGDH IKSASDLNLP FIGISLLYKN
     GFFHQRINGN GDQVVEYHEN NFATMPITPL QRNDEKVMIT VDLPGRTVYA QIWEVHVGRA
     RLYLLDTDVV ENSRSDRDIT SKLYDPTSKG RIEQEIILGV GGIRLFTALD IVPSVYHLNE
     GHSAFLLFER IRQLMLLDGV DFPTAKEIVR GNTVFTMHTP VPAGNERFEK SLVENYFRGY
     ADEMGVPWDG LWNLGHIYAE EADHLNMTVL ALQLSCKRNG VSRLHGDVSR RMWQDLWRGF
     ILSEVPVGHV TNGVHITSWL DERVRHDIEE SCSMSVHRQL LEKTDWGCLD GLDDRRLWDT
     HVALKHRLYD EVRRSIAAQW TREGEPPNRL HAFLNELNPD HLTLCFARRC TAYKRPTLIF
     HNLQRIKEIL TKADRPVNII FAGKAHPADT MGASYINLIC RLAKQDDFLG RVIFLESYDI
     RLARLLVSGA DVWLNNPTRL MEASGTSGMK AAVNGVPNCS ILDGWWDEAF DGTNGWAVGS
     GLVYQSQVNQ DIVDADNLYA TLESEVVPEF YDRGGDGVPH AWLQRMKASM QTAFRQYGTH
     RMVRDYIDDM YLPAIELSKL RAKNNNELAL GLGEWRTRIP GRFATVNIKE VKVEGISGDV
     FRLGNRLTVS AKVDRGQLLT EEIVVEFVAA TPDEETVVDC IPMQLKHTEG STLLYRATYS
     PAESGLVRYG VRVLPTHPGL ASKCDPRLIR WS
//