ID E4THX3_CALNY Unreviewed; 850 AA.
AC E4THX3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:ADR18903.1};
DE EC=2.4.1.1 {ECO:0000313|EMBL:ADR18903.1};
GN OrderedLocusNames=Calni_0992 {ECO:0000313|EMBL:ADR18903.1};
OS Calditerrivibrio nitroreducens (strain DSM 19672 / NBRC 101217 / Yu37-1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Calditerrivibrionaceae.
OX NCBI_TaxID=768670 {ECO:0000313|EMBL:ADR18903.1, ECO:0000313|Proteomes:UP000007039};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19672;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A.,
RA Brettin T., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of chromosome of Calditerrivibrio nitroreducens DSM
RT 19672.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADR18903.1, ECO:0000313|Proteomes:UP000007039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19672 / NBRC 101217 / Yu37-1
RC {ECO:0000313|Proteomes:UP000007039};
RX PubMed=21475587; DOI=10.4056/sigs.1523807;
RA Pitluck S., Sikorski J., Zeytun A., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A., Chen A.,
RA Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Brambilla E., Djao O.D., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Land M.;
RT "Complete genome sequence of Calditerrivibrio nitroreducens type strain
RT (Yu37-1).";
RL Stand. Genomic Sci. 4:54-62(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; CP002347; ADR18903.1; -; Genomic_DNA.
DR RefSeq; WP_013451116.1; NC_014758.1.
DR AlphaFoldDB; E4THX3; -.
DR STRING; 768670.Calni_0992; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; cni:Calni_0992; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_0; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000007039; 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:InterPro.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR InterPro; IPR011834; Agluc_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
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; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:ADR18903.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007039};
KW Transferase {ECO:0000313|EMBL:ADR18903.1}.
FT DOMAIN 13..122
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 608
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 850 AA; 98590 MW; B1C491A4FACFD5AC CRC64;
MKKREFFVKI NFPERLKTLE SLAYNLWWVY NNNAKDLFKM IKPELWQETL HNPIEILLSL
SEHDLKQLEK DQVFLSRLDS VWNDYIEYIK TPKWFETIRD IEKHGNMQIA YFSAEYGMHE
SIQSYAGGLG ILSGDHFKAA SDLGIPFIAV GLLYRNGYFH QYLNSDGWQL ETYPYNEFYK
MPVVEAKDEN GDPLLVEIPS YNSLIKAKIW LVHLGFSRLI LLDTDIDDNI PENKIITGKL
YDGEPEMRIK QEIVLGIGGV RALKKLGIKP TVFHINEGHP AFAVIERIKD YMVEDGLNLY
EAINMVKYST LFTTHTPVPA GFDVFDNNAI YKHLGPIYNG TPLSIDEVLK IGKVNPYSSS
EPFSMAICGV KCSIFRNGVS KLHGKVSRKI FNNLWPNVSE PFVPVGHITN GVHLQTWVAD
EIKTLFNRYL GENWYLRPYQ KSVWSNIHEI PDLELFEAKN ILRTRLVEFI RKRTINSINK
RGGSYSEIVK ANEILNPGIL TIGFARRFAT YKRGYLLFSD EERLNKILNN PKMPVQIIIA
GKAHPKDTEG KEIIKKIYHI SRKPEFRDKI VFVEDYDIQV AKYLVRGVDV WLNNPRRPME
ASGTSGMKAA INGALNFSIL DGWWVEGYKN NNGWSIGAGE EYSDPKYQDF VEGQELYDKL
ENEIVPLFYA KDRSGLPREW LKMMKNSIFI GCSEFSTSRM VMEYHEKYYT PLHELHNDLS
EQNFANLREF INFKNEISNK WHKLRIVKAE IISDNLYMGS TVKFYSEVYT DDLDPNFLKV
CVISDTNCPK IEFEDPKFIE LDLKESKDGV SIFSKEVRLT CSGKIRFAFG IFPKNRFILN
EFEDNLFVWE
//
