ID B8F9S8_DESAL Unreviewed; 434 AA.
AC B8F9S8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN OrderedLocusNames=Dalk_1323 {ECO:0000313|EMBL:ACL03024.1};
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfatibacillaceae; Desulfatibacillum.
OX NCBI_TaxID=218208 {ECO:0000313|EMBL:ACL03024.1, ECO:0000313|Proteomes:UP000000739};
RN [1] {ECO:0000313|EMBL:ACL03024.1, ECO:0000313|Proteomes:UP000000739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01 {ECO:0000313|EMBL:ACL03024.1,
RC ECO:0000313|Proteomes:UP000000739};
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
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DR EMBL; CP001322; ACL03024.1; -; Genomic_DNA.
DR RefSeq; WP_012610459.1; NC_011768.1.
DR AlphaFoldDB; B8F9S8; -.
DR KEGG; dal:Dalk_1323; -.
DR eggNOG; COG0615; Bacteria.
DR eggNOG; COG2513; Bacteria.
DR HOGENOM; CLU_027389_0_1_7; -.
DR Proteomes; UP000000739; Chromosome.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000000739};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..131
FT /note="Cytidyltransferase-like"
FT /evidence="ECO:0000259|Pfam:PF01467"
SQ SEQUENCE 434 AA; 48916 MW; 7BC7451825778226 CRC64;
MERKNVYVGM SADLVHPGHL NIINRAAELG DVTVGLLTDR AIASYKRLPF MTYEQRKTVV
ENLKNVKNVV AQETLDYVPN LKEYKPDYVV HGDDWKEGVQ SQVRQAVIDA LSEWGGELVE
VPYTLGISST QLHKVFKEIG TTPDIRRNKL RRLLNAKPLL RILEVHNGLT SLIVENISIE
NEQGRCEFDG MWSSSLTEST AKGKPDIEAV DVTARMNTLH DIMEVTTKPL IYDADTGGKI
EHFKFTVRTL ERLGVSAAII EDKVGLKKNS LFGTEVKQTQ DTIDHFCEKI RAGKAAQVTE
EFMVIARIES LILEAGMTDA VDRARAYIQA GADGIMIHSR QKEPDEIFEF CKEYKTFYRK
VPLVVIPTSY NQVTENDLAE HGINIVIYAN HLLRAAYPAM VKTAESILTH KRSKEVDFEL
FSIKNILELI PGTK
//
