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Database: UniProt
Entry: D3ACB0_9CLOT
LinkDB: D3ACB0_9CLOT
Original site: D3ACB0_9CLOT 
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
//
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