(data stored in SCRATCH zone)

SWISSPROT: E6V4B4_VARPE

ID   E6V4B4_VARPE            Unreviewed;       827 AA.
AC   E6V4B4;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 47.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   OrderedLocusNames=Varpa_0438 {ECO:0000313|EMBL:ADU34660.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34660.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34660.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34660.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
CC   -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC       carbohydrate metabolism. Enzymes from different sources differ in
CC       their regulatory mechanisms and in their natural substrates.
CC       However, all known phosphorylases share catalytic and structural
CC       properties. {ECO:0000256|RuleBase:RU000587}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-
CC         D-glucosyl](n-1) + alpha-D-glucose 1-phosphate;
CC         Xref=Rhea:RHEA:41732, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586,
CC         ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601;
CC         EC=2.4.1.1; Evidence={ECO:0000256|RuleBase:RU000587};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU000587};
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|RuleBase:RU000587}.
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DR   EMBL; CP002417; ADU34660.1; -; Genomic_DNA.
DR   RefSeq; WP_013538906.1; NC_014931.1.
DR   STRING; 595537.Varpa_0438; -.
DR   EnsemblBacteria; ADU34660; ADU34660; Varpa_0438.
DR   GeneID; 29717535; -.
DR   KEGG; vpe:Varpa_0438; -.
DR   eggNOG; ENOG4107QQN; Bacteria.
DR   eggNOG; COG0058; LUCA.
DR   HOGENOM; HOG000278444; -.
DR   KO; K00688; -.
DR   OMA; WLEMSIN; -.
DR   OrthoDB; 137158at2; -.
DR   BioCyc; VPAR595537:G1GQO-440-MONOMER; -.
DR   Proteomes; UP000008917; Chromosome.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04300; GT1_Glycogen_Phosphorylase; 1.
DR   InterPro; IPR011833; Glycg_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   PANTHER; PTHR11468; PTHR11468; 1.
DR   Pfam; PF00343; Phosphorylase; 1.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   TIGRFAMs; TIGR02093; P_ylase; 1.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; E6V4B4.
DR   SWISS-2DPAGE; E6V4B4.
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW   ECO:0000256|RuleBase:RU000587};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   Transferase {ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES     673    673       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR000460-1}.
SQ   SEQUENCE   827 AA;  92924 MW;  1BA4F7264FE09B46 CRC64;
     MTIKDFAYDH PDRDVAAFKR AVANKLIYAV GKDPVAASQD DWLNATSQAV RDQLVERWMM
     TTRANYAQDL KRVYYLSMEF LIGRTFTNAL LAVDLYDTVR EALADFGVDM SALAEREPDA
     ALGNGGLGRL AACFLDSMAT LGVPGMGYGI RYEYGMFRQR IVDGQQVETP DYWLTRGNPW
     EFQRPEVNYR VRFGGHVQKR EGTNAPYGAA DWVDTHDVLA VAYDTIIPGY GTQATNTLRL
     WSARATEEID LSAFNRGNYM GAVESKNQSE NVSRVLYPDD STPSGRELRL HQEYFFCSAS
     VQDLLRRYLR SHKTFDQLSE KVSIHLNDTH PVLAVPELMR LLLDEHGLAW DEAWAHTQKV
     FSYTNHTLMH EALETWPVEM LGRILPRHLQ IIYDMNAKFL ATVTQKVGND VELMRRLSLV
     DEAGERRVRM AYVAVLASHS INGVSGLHSE LMKQSIFADF DKIFPERFNN KTNGVTPRRW
     LAQANPPLAG LLDQRIGKGW RRDLSQLEAL KPMAAQPAFV RAFRHAKREN KLRLANWVGE
     HLKIDLDTDA MFDVQVKRIH EYKRQLLNVL HVVTRYHRIL DAQAAGTPLD IVPRVVVFAG
     KAASAYAMAK LVIRLINDVA STINADARVG KLLKVVFLPN YSVSLAEIIM PAADLSEQIS
     TAGTEASGTG NMKFALNGAL TIGTLDGANV EMRENVGPEN IFIFGNTTPE VAEIRARGYQ
     PREIYEENAD LKRVLDAIRD GAFSPGEPSR YQGIYDALVN WGDHYLLLAD YASYVAKQAE
     VDALYRDSDA WTRMAILNVA GMGAFSSDRT IAQYAHEIWN TKPVVLG
//

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