ID S9WF89_CAMFR Unreviewed; 1266 AA.
AC S9WF89;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=CB1_002050003 {ECO:0000313|EMBL:EPY74414.1};
OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY74414.1, ECO:0000313|Proteomes:UP000030684};
RN [1] {ECO:0000313|EMBL:EPY74414.1, ECO:0000313|Proteomes:UP000030684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX PubMed=23149746;
RG Bactrian Camels Genome Sequencing and Analysis Consortium;
RA Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA Bayaer T., Li Y., Meng H.;
RT "Genome sequences of wild and domestic bactrian camels.";
RL Nat. Commun. 3:1202-1202(2012).
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000256|ARBA:ARBA00037413,
CC ECO:0000256|RuleBase:RU000587}.
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:ARBA00036074};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41733;
CC Evidence={ECO:0000256|ARBA:ARBA00036074};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; KB018097; EPY74414.1; -; Genomic_DNA.
DR AlphaFoldDB; S9WF89; -.
DR Proteomes; UP000030684; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR CDD; cd12889; SPRY_PRY_TRIM67_9; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR017903; COS_domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR InterPro; IPR003877; SPRY_dom.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF26; GLYCOGEN PHOSPHORYLASE, LIVER FORM; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS51262; COS; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000030684};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT DOMAIN 115..173
FT /note="COS"
FT /evidence="ECO:0000259|PROSITE:PS51262"
FT DOMAIN 179..270
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 371..555
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT COILED 29..85
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1266 AA; 143718 MW; 5C22ABEEDBC2664B CRC64;
MLAKWPRSDK RNLRRSQLSQ ALNGLSDRAK EAKEFLVQLR NMVQQIQENS VEFEACLVAQ
CDALIDALNR RKAQLLARVN KEHEHKLKVV RDQISHCTVK LRQTTGLMEY CLEVIKENDP
SGFLQISDAL IRRVHLTEDQ WGKGTLTPRM TTDFDLSLDN SPLLQSIHQL DFVQMKATPI
LQLEECCTHN NSATLSWKQP PLSAVPAEGY ILELDDGNGG QFREVYVGKE TMCTVDGLHF
NSTYNARVKA FNKTGVSQYS KTLVLQTSEE SPWYVDVIKP KSPQRLFQWP GPAASFSNAL
SKLQRKKLRS EGLNVPQGAV TNSKFFLMMR LEKVSTVGLD MLPESGFSTH LFTGFQMITR
GHRVKGLAPS KPMPLHSRIT WLGVQSEPVA WFAFDPGSAH SDIIFSNDNL TVTCSSYDDR
VVLGKTGFSK GVHYWELTVD RYDNHPDPAF GVAHMDVMKD VMLGKDDKAW AMYVDNNRSW
FMHNNSHTNR TEGGITKGAT IGVLLDLNRK TLTFFINDEQ QGPIAFENVE GLFFPAVSLN
RNVQRVYYLS LEFYMGRTLQ NTMINLGLQN ACDEAIYQLG LDMEELEEIE EDAGLGNGGL
GRLAACFLDS MATLGLAAYG YGIRYEYGIF NQKIRDGWQI EEADDWLRHG NPWEKARPEF
MLPVHFYGRV EHTEAGAKWV DTQVVLALPY DTPVPGYLNN TVNTMRLWSA RAPNDFNLRD
FNVGDYIQAV LDRNLAENIS RVLYPNDNVA IQLNDTHPSL AIPELMRIFV DIEKLPWSKA
WEITQKTFAY TNHTVLPEAL ERWPVELVEN LLPRHLQIIY EINQKHLDKI AALFPNDVDR
LRRMSLIEEE GGKRINMAHL CIVGSHAVNG VAKIHSDIVK TQVFKDFSEL EPDKFQNKTN
GITPRRWLLL CNPGLAELIA ERIGEDYVKD LSQLTKLHSF LGDDVFLREI SNVKQENKLK
FSQFLEKEYR VKINPSSMFD VQVKRIHEYK RQLLNCLHVI TMYNRIKKDP KKLFVPRTVI
IGGKAAPGYH MAKLIIKLIT SVADVVNNDP MVGSKLKLIF LENYRVSLAE KVIPATDLSE
QISTAGTEAS GTGNMKFMLN GALTIGTMDG ANVEMAEEAG EENLFIFGMR VEDVAALDKK
GYEAKKYYEA LPELKLAIDQ IDKGFFSPKQ PDLFKDLINM LFYHDRFKVF ADYEAYVKCQ
EKVSQLYMNP KAWNTTVLKN IAASGKFSSD RTIKEYARDI WNMEPSDIKI SLSSQPSNGV
NKANGK
//
