ID I9B722_9FIRM Unreviewed; 433 AA.
AC I9B722;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN ORFNames=FB4_1779 {ECO:0000313|EMBL:EIW20927.1};
OS Pelosinus fermentans B4.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW20927.1, ECO:0000313|Proteomes:UP000004324};
RN [1] {ECO:0000313|EMBL:EIW20927.1, ECO:0000313|Proteomes:UP000004324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:EIW20927.1,
RC ECO:0000313|Proteomes:UP000004324};
RX PubMed=22933770; DOI=10.1128/JB.01174-12;
RA Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL J. Bacteriol. 194:5147-5148(2012).
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:EIW20927.1}.
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DR EMBL; AKVJ01000002; EIW20927.1; -; Genomic_DNA.
DR RefSeq; WP_007930206.1; NZ_AKVJ01000002.1.
DR AlphaFoldDB; I9B722; -.
DR PATRIC; fig|1149862.3.peg.54; -.
DR OrthoDB; 9802794at2; -.
DR Proteomes; UP000004324; Unassembled WGS sequence.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0050188; F:phosphoenolpyruvate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd02170; cytidylyltransferase; 1.
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; 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; PTHR43793; FAD SYNTHASE; 1.
DR PANTHER; PTHR43793:SF1; FAD SYNTHASE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Pyruvate {ECO:0000313|EMBL:EIW20927.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..131
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 433 AA; 48052 MW; D47AD26A578271A4 CRC64;
MTKKVYVGMS ADLIHPGHLN IIKEAQKLGE VIVGLLTDKA IASYKRLPYL DYEQRRIIVE
NIKGVNQVIP QETLDYIPNL TQIKPDFVVH GDDWKTGVQK EVRARVIDVL KEWGGELVEI
GYTQGISSTK LNQHLKEIGT TPAIRMKRFK RLLQSKPIVR LMEAHNGLTG LIVENTQINI
DGATKEFDGM WLSSLTDSTA KGKPDIECVD VTSRMNTIND ILEVTTKPII FDGDTGGITE
HFVFTVKSLE RLGVSAVIIE DKIGLKKNSL FGTDVVQTQD SIENFSHKIA SGKKAQVTED
FMIIARVESL ILKNGINDAV TRAKAYIAAG ADGIMIHSKE KSPAEILEFC SIYKTLENRV
PLIIVPSSYN SVYENELIAA GANVVIYANH LLRSAYPAMI ETAQSILRHG RSLECDQKVM
PIREILTLIN GGE
//
