ID D3ACB0_9CLOT Unreviewed; 669 AA.
AC D3ACB0;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN Name=aepX {ECO:0000313|EMBL:EFD00588.1};
GN ORFNames=CLOSTHATH_01238 {ECO:0000313|EMBL:EFD00588.1};
OS Hungatella hathewayi DSM 13479.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=566550 {ECO:0000313|EMBL:EFD00588.1, ECO:0000313|Proteomes:UP000004968};
RN [1] {ECO:0000313|EMBL:EFD00588.1, ECO:0000313|Proteomes:UP000004968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13479 {ECO:0000313|EMBL:EFD00588.1,
RC ECO:0000313|Proteomes:UP000004968};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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:EFD00588.1}.
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DR EMBL; ACIO01000079; EFD00588.1; -; Genomic_DNA.
DR RefSeq; WP_006771780.1; NZ_GG667619.1.
DR AlphaFoldDB; D3ACB0; -.
DR HOGENOM; CLU_410410_0_0_9; -.
DR Proteomes; UP000004968; Unassembled WGS sequence.
DR GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR012698; PEnolPyrv_PMutase_core.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR NCBIfam; TIGR02320; PEP_mutase; 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR42905:SF7; PHOSPHOENOLPYRUVATE PHOSPHOMUTASE-RELATED; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR Pfam; PF12804; NTP_transf_3; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EFD00588.1};
KW Pyruvate {ECO:0000313|EMBL:EFD00588.1}.
FT DOMAIN 3..114
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
FT DOMAIN 248..342
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 669 AA; 75603 MW; 63CAB0604E0AF589 CRC64;
MKALILNSGL GKRMGSLTSE HPKCMSEISS RETIISRQLK QIANAGIEEV VITTGMFDTT
LINYCQSLEL PLHYTFVKNP LYQETNYIYS IYCAREYLDD DIIMMHGDLV FENLVFDAIL
ESPKSCVAVS STIPLPEKDF KAVVRENRVL QIGTEFFNEA VAAQPLYKLL KNDWKIWLNH
IDVFCKQKNV SCYAEQAFNE VSDHCRIAPI DIENLLCNEI DNPEDLAVVS SKLREVENRT
VYICFSTDML HSGHIAIIKK AQHFGKLIIG VLSDEAVVSY KRFPLLPFNE RKTIFENILG
VYKVVGQKTL SYKENIKKYK PTYVVHGDDW VSGFQKPVRD EVVSALAEYG GKLVEFPYSN
DEKYQILENR ARADLSLPDI RRIRLKKSIQ MKGTVTAIEA HSGITGLIAE KTVVYQNGEA
HQFDAMWVSS LCDSTAKGKP DIELVDMTSR LRTIDDIMEV TTKPIIFDGD TGGMTEHFVY
TVKTLERMGV SMIIIEDKTG LKRNSLFGTE VKQTQDSIQN FCAKIKAGKN AQKTKDFMIC
ARIESLILDQ SMDDALERAF AYIGAGADAI MIHSRKKDPT EIFEFIANFR SKNQTTPLVV
VPTSFNAVTE EEFKQRGVNI VIYANQLTRS GFPAMQQAAR TILENHRAKE CDDICMPIKD
IITLIPADV
//