ID H1Q4J8_9BACT Unreviewed; 852 AA.
AC H1Q4J8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=DUF3417 domain-containing protein {ECO:0000259|Pfam:PF11897};
GN ORFNames=HMPREF9140_01836 {ECO:0000313|EMBL:EHO67099.1};
OS Prevotella micans F0438.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=883158 {ECO:0000313|EMBL:EHO67099.1, ECO:0000313|Proteomes:UP000016023};
RN [1] {ECO:0000313|EMBL:EHO67099.1, ECO:0000313|Proteomes:UP000016023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0438 {ECO:0000313|EMBL:EHO67099.1,
RC ECO:0000313|Proteomes:UP000016023};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA Blanton J.M., Wade W.G., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella micans F0438.";
RL Submitted (DEC-2011) 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}.
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:EHO67099.1}.
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DR EMBL; AGWK01000049; EHO67099.1; -; Genomic_DNA.
DR RefSeq; WP_006953403.1; NZ_JH594523.1.
DR AlphaFoldDB; H1Q4J8; -.
DR STRING; 883158.HMPREF9140_01836; -.
DR PATRIC; fig|883158.3.peg.1839; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_10; -.
DR Proteomes; UP000016023; Unassembled WGS sequence.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016023}.
FT DOMAIN 22..123
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 852 AA; 98370 MW; 89D75B27A4086D80 CRC64;
MKIKSDYANE PRWKEVNVKS SLPKEMESLD KLAHNMWWSW NYQARNMFKS LDEKLYEEVG
HNPVLLLERL SYERKEAIVK DKELMKRVKE VYKLFTEYMS VKPDTKRPSV AYFSMEYGIN
QVLKIYSGGL GMLAGDYLKE ASDSNVDLCA VGFLYRFGYF TQSLSMDGQQ IAKYDAQNFN
SLPIERVLDK DGNQVVVDVP YNGYQVHALV WVANVGRIKL YLLDTDNDMN SEFDRPITHT
LYGGDWENRI KQEILLGIGG ILTLKKLGIK KDIYHCNEGH AALCNLQRLC DYIDQGLTFN
QAMELVRASS LYTVHTPVPA GHDYFDEELF GKYMGAYPEK LGISWDEFIG MGRTNPDDHS
ERFCMSTFAC NTSQEINGVS KLHGWVSQKM FAPLWKGYFP EENNVGYVTN GVHLPTWTAT
EWRKVYDEYF DSSFISDQSN EKIWHAIYNV PDEIIWNTRM ALKKKLIKYI RDKFTQQWLR
NQGDPAKVVS ILERINPNAL MIGFCRRFAT YKRAHLLFTD LERLERIVND PEHPVLFFFS
GKAHPADGAG QGLIKRIFEI SRMPQFLGKI IFLEDYDMQL ARRLVSGVDI WMNTPTRPLE
ASGTSGEKAE MNGVVNLSVL DGWWVEGYRE GAGWALPQER TYENQTYQDQ LDAATIYSLL
ENEIVPLYFN KTEKRDYSAD WVGVVKNSIA SIAPHYTMKR QLDDYYSKFY EKEAQRSKKL
HANDNRLAKE IALWKETVAE RWDSIHVVSK NIDELQDVVT GRKTHLTYVI DEQGLNDAIG
LEFVVLNSDP SAEQSVHEVI PFKLVKAEGN LYTFEVAFEP DAAGAFKCAV RMFPKSKLLA
HRQDFAYVKW LD
//
