ID A0A1J1HGT9_9DIPT Unreviewed; 885 AA.
AC A0A1J1HGT9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU004511, ECO:0000256|RuleBase:RU366077};
DE Includes:
DE RecName: Full=Phosphoglycerate mutase {ECO:0000256|RuleBase:RU004511};
DE EC=5.4.2.11 {ECO:0000256|RuleBase:RU004511};
DE EC=5.4.2.4 {ECO:0000256|RuleBase:RU004511};
DE Includes:
DE RecName: Full=Leishmanolysin-like peptidase {ECO:0000256|RuleBase:RU366077};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366077};
GN ORFNames=CLUMA_CG000834 {ECO:0000313|EMBL:CRK87091.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK87091.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK87091.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000256|RuleBase:RU004511};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-
CC bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000505,
CC ECO:0000256|RuleBase:RU004511};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601577-2,
CC ECO:0000256|RuleBase:RU366077};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR601577-2,
CC ECO:0000256|RuleBase:RU366077};
CC -!- SIMILARITY: Belongs to the peptidase M8 family.
CC {ECO:0000256|ARBA:ARBA00005860, ECO:0000256|RuleBase:RU366077}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717,
CC ECO:0000256|RuleBase:RU004511}.
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DR EMBL; CVRI01000003; CRK87091.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J1HGT9; -.
DR STRING; 568069.A0A1J1HGT9; -.
DR OrthoDB; 24037at2759; -.
DR Proteomes; UP000183832; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.10.170.20; -; 1.
DR Gene3D; 3.90.132.10; Leishmanolysin , domain 2; 1.
DR Gene3D; 2.10.55.10; Leishmanolysin domain 3; 1.
DR Gene3D; 2.30.34.10; Leishmanolysin domain 4; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001577; Peptidase_M8.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR NCBIfam; TIGR01258; pgm_1; 1.
DR PANTHER; PTHR10942; LEISHMANOLYSIN-LIKE PEPTIDASE; 1.
DR PANTHER; PTHR10942:SF0; LEISHMANOLYSIN-LIKE PEPTIDASE; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF01457; Peptidase_M8; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU004511};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366077};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU004511};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601577-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|PIRSR:PIRSR601577-2};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366077};
KW Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601577-2}.
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 467
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-1"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 188..189
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 466
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 470
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 573
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT SITE 187
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 885 AA; 101462 MW; 4FA8D2F6267A6B4D CRC64;
MAKYKIVMVR HGESEWNQLN LFCGWYNAEL SDKGRQEALD AGKAIKDAGL KFDLAHTSVL
KRANITLDSI LQESGQTGIP IQKTWRLNER HYGGLTGMNK SETAEKYGEK QVQIWRRSFD
TPPPPMEPDH KYYKIIVEDS IYKDGPSKEE FPMFESLKLT IQRTLPYWND VIIPQLKEGK
KIIIAAHGNS LRGIVKHLDQ MSDEAIMGLN LPTGIPFVYE LDENFKPVVS MQFLGDPETV
RKAMESVANQ GKAKHHCNHE HPKAHEVIHG VHLGEAEHII KKRSIDQPLR ILMFYDESVY
RLDEEKFQLI NNTILPEAVS FWEKALYVRE TKETIRLNRK CESTQVFIKN SLTHCIDQCK
PITMCGEVQV PEEHLDVCRV CNATGQNCRS DSNSKVGAGI VGADFVFYVS ARQTERCHKG
LTVGYAAHCQ QESSLDRPIA GHANLCPDSI STKPQELQTL LSTVKHEILH ALGFSVSLYA
FFRDENGEPR TPRKPDTGKP FLNEKLQIHQ WSNKTIQRIV RNNWAVRNGV IKKNIDMMVT
PRVVGEVRKH FNCSELEGAE LEDQGGEGTA LTHWEKRVFE AEAMSGTHSS RPVFSRITLA
LMEDTGWYKA NYEMASDLTW GKNLGCDFVM KSCKSWITSH HNNGRSIHPF CSKIKRDPLQ
TECTDDRNSV ALCNLVKHEY PLPKEYQNFD SLNHVHEDLE YYGGSVSLAD HCPYIQEFTW
RSKNVVVRGS QCKFEENNPH HEKNFALEKY GRESKCFEHS ERMWEERSCQ QTREWQHWGS
GCYTYSCSNG RLHIHVSNYT FECFHPGQEL NIRILENNWL HHGAIICPSC HELCDNFFAS
TTGETCKTPE EAPSSYFYPK DNLRCRANVL TPTILILVAF TFIRL
//