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Database: UniProt
Entry: C5NZE6_COCP7
LinkDB: C5NZE6_COCP7
Original site: C5NZE6_COCP7 
ID   C5NZE6_COCP7            Unreviewed;      1403 AA.
AC   C5NZE6;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Glycogen debranching enzyme {ECO:0000256|ARBA:ARBA00020723};
DE            EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560};
DE            EC=3.2.1.33 {ECO:0000256|ARBA:ARBA00012778};
DE   AltName: Full=Glycogen debrancher {ECO:0000256|ARBA:ARBA00031477};
GN   ORFNames=CPC735_011570 {ECO:0000313|EMBL:EER29839.1};
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929 {ECO:0000313|EMBL:EER29839.1, ECO:0000313|Proteomes:UP000009084};
RN   [1] {ECO:0000313|EMBL:EER29839.1, ECO:0000313|Proteomes:UP000009084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- FUNCTION: Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-
CC       alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase
CC       in glycogen degradation. {ECO:0000256|ARBA:ARBA00003530}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in
CC         glycogen phosphorylase limit dextrin.; EC=3.2.1.33;
CC         Evidence={ECO:0000256|ARBA:ARBA00000927};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC         position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC         glucan.; EC=2.4.1.25; Evidence={ECO:0000256|ARBA:ARBA00000439};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the glycogen debranching enzyme family.
CC       {ECO:0000256|ARBA:ARBA00025780}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EER29839.1}.
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DR   EMBL; ACFW01000001; EER29839.1; -; Genomic_DNA.
DR   RefSeq; XP_003071984.1; XM_003071938.1.
DR   GeneID; 9697479; -.
DR   KEGG; cpw:CPC735_011570; -.
DR   VEuPathDB; FungiDB:CPC735_011570; -.
DR   HOGENOM; CLU_001517_2_0_1; -.
DR   OrthoDB; 1427975at2759; -.
DR   Proteomes; UP000009084; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004135; F:amylo-alpha-1,6-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0005980; P:glycogen catabolic process; IEA:InterPro.
DR   CDD; cd11327; AmyAc_Glg_debranch_2; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR010401; AGL/Gdb1.
DR   InterPro; IPR032788; AGL_central.
DR   InterPro; IPR032792; AGL_glucanoTrfase.
DR   InterPro; IPR032790; GDE_C.
DR   InterPro; IPR006421; Glycogen_debranch_met.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   NCBIfam; TIGR01531; glyc_debranch; 1.
DR   PANTHER; PTHR10569; GLYCOGEN DEBRANCHING ENZYME; 1.
DR   PANTHER; PTHR10569:SF2; GLYCOGEN DEBRANCHING ENZYME; 1.
DR   Pfam; PF06202; GDE_C; 1.
DR   Pfam; PF14701; hDGE_amylase; 1.
DR   Pfam; PF14702; hGDE_central; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Transferase {ECO:0000313|EMBL:EER29839.1}.
FT   DOMAIN          1..442
FT                   /note="Glycogen debranching enzyme glucanotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF14701"
FT   DOMAIN          597..840
FT                   /note="Glycogen debranching enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF14702"
FT   DOMAIN          923..1384
FT                   /note="Glycogen debranching enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06202"
SQ   SEQUENCE   1403 AA;  159123 MW;  0F13BA2F4D8736C8 CRC64;
     MPVESLSIFS IVSKFMGKFP ADWNKHLQGI GQRGYNVVHF TPLMTRGASN SPYSIYNQLE
     FDRQCFPNGE SDVIDMVTRM EKEYGLLALT DVVWNHTAHN SKWLQEHPEA GYNVETAPWL
     EAALELDDAL LSYGNALQSL DLPTEFKTVE DLVSVMQQMR PHVIEKIKLW EFYSVNVQRD
     TEAIIKAWKS GNLDYPKGGF GEVGVGGLSE IRQWPFEKKA AFLREKALEN DNQILGRYSR
     KVNPRIGAAL ITALYGRYDE TTADIPVVEE NVFKTLDSLN LPLFREFDDD VSEIFDQLFH
     RIKYLRLDDH GPKLGPVTPK NPLVETYFTR LPLNDITKAH SPRSLALVNN GWVWNADALR
     DNAGPGCRAY LKREVIVWGD CVKLRYGNCP EDNPFLWDYI TRYTKLMAKH FAGFRIDNCH
     STPLPVAEYL LHEARRIRPN LMVYAELFTG SEKVDYLFTK RLGLTALIRE AMQAWSAAEL
     SRLVHRHGGL PIGSFDPSLL SHWCQMETKV VLHHIRPTTV HALFMDCSHD NETPAQKRDP
     RDTLPNAALV AMCASAIGSV MGYDEIYPEH VNLVTETRSY HSVFSENGVQ DATGEGGIGG
     IKKLLNSLHT EMAIDEYDET HIHHDAEYIT VHRVHPHTRK GTLLISRTAF SASNVKHILA
     PIHLTGTKAS LLGAWKLEVE NDTEAKRIVA ADEKYLRGLP SRVSEISGFR LEENGDDTII
     YTPDDFPPGS IALLKTHIHE RDLPVDLSKF ITADADATFR SVDLTGLNFT LYRCDSEERD
     SSGGKDGVYK IPNFGPLVYA GLQGWWSVLE EIIKTNDLGH PLCDNLRAGQ WALDFVVGRM
     RRAITQQGYS QLEGPTKWLE DRFNAVRRVP NFLLPRYFTI IIKAAYDAAC RHAIHCLGVI
     IEHGQHFIHE LALVSVQHLG EVKSASLYPT NQVPCLAAGL PHFATDWARC WGRDVFISLR
     GLLLATGRFD DAKEHILAFA STLKHGMIPN LLSSGKFPRY NSRDSVWFFL QAIQDYTHIV
     PNGIRILEEN VPRRFLPYDD TWFPFDDKRA YSRSSTIAEI IQEVFQRHAS GISYREHNAG
     PELDLQMKPE GFQVDVHVDW ETGIIFGGNQ WNCGTWMDKM GESVKAKNQG YPGTPRDGAP
     IEISGLLYSA LRWVSDLRRK GHYPYSGVDI ESGLTITFDD WATRVKTHFE KCYYVPVDSE
     EDRDFNVDSK LVNRRGIYKD IYKSSQPYED YQLRPNFTIA MTVAPDLFDA ERGFHALTIA
     DVVLRGPLGM ATLDPTDLNY RPYYNNSEDS TDFATSKGRN YHQGPEWLWP TGYFLQALLK
     FSLLRNSSHQ SLMDISQQIT MRLERCCKSL RESTWKGLTE LTNKNGEFCV DSSPTQAWSA
     ACLLALYYDA SEIQKARSAS LSV
//
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