ID   B8J4C2_DESDA            Unreviewed;      1421 AA.
AC   B8J4C2;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:ACL48380.1};
DE            EC=2.4.1.1 {ECO:0000313|EMBL:ACL48380.1};
DE            EC=2.4.1.11 {ECO:0000313|EMBL:ACL48380.1};
GN   OrderedLocusNames=Ddes_0468 {ECO:0000313|EMBL:ACL48380.1};
OS   Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL48380.1};
RN   [1] {ECO:0000313|EMBL:ACL48380.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27774 {ECO:0000313|EMBL:ACL48380.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT   ATCC 27774.";
RL   Submitted (JAN-2009) 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; CP001358; ACL48380.1; -; Genomic_DNA.
DR   STRING; 525146.Ddes_0468; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   KEGG; dds:Ddes_0468; -.
DR   eggNOG; COG0058; Bacteria.
DR   eggNOG; COG0438; Bacteria.
DR   HOGENOM; CLU_005051_0_0_7; -.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR   GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 5.
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   Glycosyltransferase {ECO:0000313|EMBL:ACL48380.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACL48380.1}.
FT   DOMAIN          578..683
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
SQ   SEQUENCE   1421 AA;  159830 MW;  8DA49F752B8E8010 CRC64;
     MNFNSSLVTL FEVSWEVCNK VGGIHSVVTS KALQAVEHFG EDYFLLGPAL KNNPGFEETD
     EHAWDSLRMG LATRDLKCRL GRWNIPGRPK VILVEFDKRY SSNQLLFEMW KNYGVDSLSG
     GWDYIEPIMF ATACGEVIAT IHESRVEPMQ GRSVALFHEW MCGAGLLTVK KLTPEVGTVF
     TTHATTLGRA MAGTGRDIYT NMRNINPANE AAALNITAKW SMESAAAREA DAFTTVSPIT
     GEESTVFLGR QPDVITTNGL DLRVIPDYTD DREVPSATRA KIMSAAGRFL RGSLPEHTRI
     FTISGRYEMH NKGVDIFLEA LARADRNLSG TNSSILALCL VMGGHTGVNA AAVSGNPDDT
     DNGMPFICTH RVWNAPQDPI INACRRLGLD NREERRVKVI FVPAMLDGHD GFFDIPYEEI
     LAACDMGFFP SWYEPWGYTP QESAAWAVPT LTTDLSGFGM WAREQMKEES MDRTGVCVMP
     RRGMSFDQSV DRLHERVLGA AACPEGELCS WRGHARDLAE KTSWSYFFDN YIKAFDIALA
     KSDARTDHDS AHGALTRVLT ASCSATPFLR PIMAVAEVPH ELSRLRELAQ NIWWSWHDQA
     KALFMALNPQ LWEACRNPLK MLEEAWPARL KELIANEEYM AMYHKVMDRF DAYMAEPIRS
     LSVDVTPEHP IVYFSTEYGL NESVPIYSGG LGVLSGDHLK SASDMALPLV GIGLLYKSGY
     FMQEIDSSGR QVAQYPVNNF GQMPIKQVHD AQGQPVYIQL ELPGRILYAR VWRLQVGRIS
     LYLMDTDTSR NTDEDRRITD RLYEANRETR LLQEILLGQG GMRLLRTLGI VPGVYHMNEG
     HSAFMALERV RDCMTQGMSH DEAVVRVRSN TLFTTHTPVP AGNESFSLEL MERYFSGMAK
     NLDLSWQQFV QLGQIEGGDS HAFEMTVLAL RLSCWANGVS RLHGVVSRHM WNNLWKGLPT
     AETPIGHVTN GVHTPSYVGS WMHELLHKHL GAGWLQALPG STVWDKVDDI PDEAFWAARQ
     HQKEALLDAL RKRIPVFAQR FKLDAAVRKR MEALLRPETL IIGFARRFAP YKRATLLFAD
     PDRLARILNN PHRPVVLVFS GKAHPADEAG INLIQEVMRM CQDERFLGRI FFLENYSLSV
     SRIMSQGCDV WLNTPRRPHE ASGTSGMKLP VNGGINLSIS DGWWCEGYNR QNGWTIGPVV
     TTELPSNEQN DYADAEALYN LLENAVLPLY FDRTQGDLPT QWIAMAKRSF KSLTAMYGSN
     RMLNDYIRQY YLRAARRRNM LAENDWSACR RLAAWEKDLP ARFGTVKVEE LFISGVENNT
     MICGEPVSVR LHMHLGEMQP EEILVQLVIG RALVNGSFID KPEILRLEPR AADHNGESGN
     GMNYAATYIP THSGQYRYGV RVLPYHKNLA TPLETGLVLW A
//