ID A0A151XBW0_9HYME Unreviewed; 941 AA.
AC A0A151XBW0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU000587, ECO:0000256|RuleBase:RU363132};
DE Includes:
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
DE Includes:
DE RecName: Full=Reticulon-like protein {ECO:0000256|RuleBase:RU363132};
GN ORFNames=ALC60_03209 {ECO:0000313|EMBL:KYQ57852.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ57852.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ57852.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ57852.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ57852.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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|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|RuleBase:RU000587};
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: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363132}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU363132}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; KQ982316; KYQ57852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151XBW0; -.
DR STRING; 64791.A0A151XBW0; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; 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: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; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 1.20.5.2480; -; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR003388; Reticulon.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF13; GLYCOGEN PHOSPHORYLASE, MUSCLE FORM; 1.
DR Pfam; PF00343; Phosphorylase; 2.
DR Pfam; PF02453; Reticulon; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS50845; RETICULON; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU363132};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363132};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW Transferase {ECO:0000256|RuleBase:RU000587};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363132};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363132}.
FT TRANSMEM 74..90
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363132"
FT TRANSMEM 179..207
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363132"
FT DOMAIN 61..232
FT /note="Reticulon"
FT /evidence="ECO:0000259|PROSITE:PS50845"
SQ SEQUENCE 941 AA; 107709 MW; F922D613042EFDDC CRC64;
MADLDSATYP AVTKNVDEGN EVCKRSSADA NSASMTNSNP CFWNILNPHA WFNPERLNPK
VAALIYWRDP KKSGIVFGTI LGVLLSLAYF SLISVLAYMS LLALSGTIIF RIYKTVLQAV
QKTSDGHPFK DILDLDLTLP AEKVHEVADV AVAHANAAVS ELRRLFLVED FVDSLKFSVL
LWCLTYVGSW FNGMTLIIIG VVALFTLPKV YETNQEQIDQ NLALVQTKFS EITTKHLHYT
LVKDRNVATS RDYFFALAHS VKDNLVSRWI RTQQHYYEKD PKRVYYLSLE YYMGRSLQNT
MINLGIQGAC DEAMYQANIE ELEELEEDAG LGNGGLGRLA ACFLDSMATL GLAAYGYGIR
YEYGIFAQKI KNGEQIEEPD DWLRYGNPWE KARPEFMLPV NFYGHVIDTS EGKKWVNTQV
IFAMPYDSPI PGYKNNVVNT LRLWSAKSPI EFNLKFFNDG DYIQAVIDRN LAENISRVLY
PNDNFFEGKE LRLKQEYFMV AATLQDIIRR YKSSKFGSRE HHRTDFKAFP DKVAIQLNDT
HPSLAIPELM RILIDVERLS WEEAWDITTR TCAYTNHTVL PEALERWPTH MLESILPRHL
QIIYEINHLH LQNVAAKWPG NMDRIRQMSL VEEEGEKRVN MAHVSIVGSH AINGVARIHS
EILKDSVFRA FYELTPEKFQ NKTNGITPRR WLLLCNPNLS DIIEEKIGSE WTVHLEQLEQ
LKKWAKDPVF QRNVVKVKQE NKLRLAQALE KEYGVRVNPA SIFDIQVKRI HEYKRQLLNC
LHVITLYNRI KKDPSAYFVP RTVMIGGKAA PGYHLAKKII KLICSVANVI NNDPIVGDKL
KLIFLENYRV TLAEKIIPAA DLSEQISTAG TEASGTGNMK FMIMELCFIF DETKWVEMAI
HNIASSGKFS SDRTIAEYAR EIWGVEPNWQ KLPDPHEPRD I
//
