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Database: UniProt
Entry: A1K909_AZOSB
LinkDB: A1K909_AZOSB
Original site: A1K909_AZOSB 
ID   A1K909_AZOSB            Unreviewed;       434 AA.
AC   A1K909;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=phosphoenolpyruvate mutase {ECO:0000256|ARBA:ARBA00024063};
DE            EC=5.4.2.9 {ECO:0000256|ARBA:ARBA00024063};
GN   Name=pepM {ECO:0000313|EMBL:CAL95314.1};
GN   OrderedLocusNames=azo2698 {ECO:0000313|EMBL:CAL95314.1};
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=418699 {ECO:0000313|EMBL:CAL95314.1, ECO:0000313|Proteomes:UP000002588};
RN   [1] {ECO:0000313|EMBL:CAL95314.1, ECO:0000313|Proteomes:UP000002588}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72 {ECO:0000313|EMBL:CAL95314.1,
RC   ECO:0000313|Proteomes:UP000002588};
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT   strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(2006).
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DR   EMBL; AM406670; CAL95314.1; -; Genomic_DNA.
DR   RefSeq; WP_011766424.1; NZ_CP016210.1.
DR   AlphaFoldDB; A1K909; -.
DR   STRING; 62928.azo2698; -.
DR   KEGG; aoa:dqs_2833; -.
DR   KEGG; azo:azo2698; -.
DR   eggNOG; COG0615; Bacteria.
DR   eggNOG; COG2513; Bacteria.
DR   HOGENOM; CLU_027389_0_1_4; -.
DR   OrthoDB; 9771433at2; -.
DR   Proteomes; UP000002588; 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; 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, ECO:0000313|EMBL:CAL95314.1};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002588};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          11..132
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
SQ   SEQUENCE   434 AA;  48543 MW;  6A67705823A475ED CRC64;
     MKTKIVYVGM SADLVHSGHL NIIRHAASLG EVVIGLLTDK AIASYKRIPY MPFEQRMAVV
     ENIKGVSRVV PQTTLDYTPN LELLKPDYVV HGDDWREGVQ RETRQKVIDT LKQWGGELVE
     IPYTAGISST RLQAAIKEIG TTPDIRRSAL RRLLQVKPLI RFLDIHNALS GLIIEHTAVD
     TPSGRREFDG MWGSSLTDST AKGKPDIEAV DVSARVQTLN EVLEVTTKPI IYDGDTGGQP
     EHFNFTVRTL ERLGISAIVI EDKTGLKRNS LFGNDVPQTQ ESIENFCNKI RTGKRAQATD
     EFMIIARIES LILDKGVDDA IERAQAYLAA GADGIMIHSR KTTPDEIFAF CERYRQLENR
     KYLVAVPSTY NTVTEEELQQ RGVNIVIYAN HLLRSAYPAM VETARCILEH HRSSECDARL
     LPINDILALI PGTR
//
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