ID L1PBY3_9FLAO Unreviewed; 1412 AA.
AC L1PBY3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Alpha-glucan phosphorylase {ECO:0000313|EMBL:EKY13229.1};
GN ORFNames=HMPREF9075_00113 {ECO:0000313|EMBL:EKY13229.1};
OS Capnocytophaga sp. oral taxon 332 str. F0381.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1127692 {ECO:0000313|EMBL:EKY13229.1, ECO:0000313|Proteomes:UP000010419};
RN [1] {ECO:0000313|EMBL:EKY13229.1, ECO:0000313|Proteomes:UP000010419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0381 {ECO:0000313|EMBL:EKY13229.1,
RC ECO:0000313|Proteomes:UP000010419};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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:EKY13229.1}.
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DR EMBL; AMET01000007; EKY13229.1; -; Genomic_DNA.
DR STRING; 1127692.HMPREF9075_00113; -.
DR PATRIC; fig|1127692.3.peg.108; -.
DR eggNOG; COG0058; Bacteria.
DR eggNOG; COG0297; Bacteria.
DR HOGENOM; CLU_005051_0_0_10; -.
DR Proteomes; UP000010419; Unassembled WGS sequence.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 4.
DR InterPro; IPR011834; Agluc_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR InterPro; IPR008631; Glycogen_synth.
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; PF05693; Glycogen_syn; 2.
DR Pfam; PF00343; Phosphorylase; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000010419};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 581..682
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
SQ SEQUENCE 1412 AA; 161839 MW; 219D8D50A3B5507A CRC64;
MSEKKLNPDY VFETSWEVCN KVGGIYTVIA TKVPSIAKKF RSKYILIGPD IWQHTENKEF
VENPNLFKSW RTKAAAEGLR IRVGNWKIEG EPIVILVDFS HYVSNKNEIL RFYWDAYKLD
SFGSSWDYVE SMLFGYAAGK VIESFVKFNT ASRENVICHF HEWMTASGLL YLENTMPKIG
SVFTTHATVL GRAIAGNGYP LYNEIKNYNP KDMAYKLGVQ HKHFVERQAA KTADCFTTVS
EITAQEAYHF LGRRTDMITP NGFDDKIIPA PKELAKKRTE AKSKLIAVAE ALIAEPIGQN
TKIVAISGRY EFHNKGIDAF IDALGVLNRN TKNKENVLAY ILIPTGHDAP HQGLLNNLAN
PEQKIANEQK HLTHILPDVY HDQIMNRIYE QKLFNGKNDK VKVVFCPSYL NGNDGVFNLS
YYDLLTGIDG TVFPSYYEPW GYTPLESLAF SVPTITTSLA GFGKWVNSYY PSEQNAIQVV
ERNDSNYGDV VAAIVKNITD LLAISNADLD KQRKQANEVS QIALWKNLVQ HYIKAYELTL
ENIEDRVEKL PFVQTDGLAY LEKMKVVNTP NWRSVIIHRA IPEALQPLEE LSKNLWWCWN
DEAYEVFKYV DSEKWIEVRK NPIALLDSIS LKRYKELEQD STFMRNLSKV YADFQAYMAK
KAEMTSPSVS YFSMEYGLHS SLKIYSGGLG ILAGDYLKEA SDKATKITGV GLLYRYGYFT
QKLSSAGNQE ADYEAQDFSK IPVSPVFDAE GKWIIVSLPL PHRTLYARVW RVDVGRIELY
LLDTDFENNR EDDRSITHHL YGGNWENRLK QEMLLGLGGI QMLRKLGINS DVYHCNEGHA
AFIGLERLSE YIEKDHLSFS EAMEVVRASS LFTTHTPVPA GHDAFEEGLL RAYLGNYTER
LHVNWEQILA LGKINLADPH EKFSMSNLAA NLSQEVNGVS WLHGEVSKDI LKDLWPGYMP
EELHISYVTN GVHQPTWTAG LWKDVENEVF GKDYQTHHYD PKGFEGIYKV SDKRVWEIKN
ALRSKLLRRI EQKLRLEKNT PYFSPRQLVE IKENLREDIL TIGFARRFAT YKRAHLLFTN
IERLDRIVNN PERPVQFVFA GKAHPADKAG QDLIKNIVEI SKLPQFLGKI LFIPNYDMEL
ARHMVQGVDV WMNTPTRPLE ASGTSGEKAA MNGVMHFSVL DGWWVEGYRE DAGWALPMER
AYENQQYQNE MDAEMIYNII EDEIAPIFYD KNKEGISTRW CALIKNTIAK VAVNFTTTRM
LTDYENQYYY PMTERVNKLK DNEFAIAIQL ADWKRKVTQE WDNIKVLDIR VPNRNEQLIS
IGKTYKGEVD LEVGELSPED VGVELVVAEH KDDKLKVLSK TEFPLVHTEG NKGTYRLEIA
SEYPGALQLA IRIFPKNSLL PHRQDFALVK WL
//