ID A0A0J7XLY7_9SPHN Unreviewed; 325 AA.
AC A0A0J7XLY7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Carboxyvinyl-carboxyphosphonate phosphorylmutase {ECO:0000313|EMBL:KMS52986.1};
GN ORFNames=V473_18490 {ECO:0000313|EMBL:KMS52986.1};
OS Sphingobium cupriresistens LL01.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1420583 {ECO:0000313|EMBL:KMS52986.1, ECO:0000313|Proteomes:UP000052232};
RN [1] {ECO:0000313|EMBL:KMS52986.1, ECO:0000313|Proteomes:UP000052232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL01 {ECO:0000313|EMBL:KMS52986.1,
RC ECO:0000313|Proteomes:UP000052232};
RX PubMed=25850427; DOI=10.1534/g3.114.015933;
RA Pearce S.L., Oakeshott J.G., Pandey G.;
RT "Insights into Ongoing Evolution of the Hexachlorocyclohexane Catabolic
RT Pathway from Comparative Genomics of Ten Sphingomonadaceae Strains.";
RL G3 (Bethesda) 5:1081-1094(2015).
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:KMS52986.1}.
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DR EMBL; JACT01000005; KMS52986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7XLY7; -.
DR STRING; 1420583.V473_18490; -.
DR PATRIC; fig|1420583.3.peg.3494; -.
DR Proteomes; UP000052232; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProt.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR42905:SF7; PHOSPHOENOLPYRUVATE PHOSPHOMUTASE-RELATED; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000052232}.
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 325 AA; 34731 MW; 487EFF926C3A0878 CRC64;
MDGDIRRRRD RQVGHAIDRR TGPGRRCPPL CVGRHHPAQL HGAGVRRMIA FDTLSTTGRP
LVLPGAHDAL SARMIEAAGF SAYGVGGSAL AAVQLALPDA GLQSFGEYRD AVARIMEGST
LPLMVDGENG FGDAKATVRT VRSFEKLGAA AIAFEDLVLP PRLDRLPAIS TREEIQGKLR
AALAARQSDA FQIVGRSDAA YAVDLDEAIL RAASYQTLGV DAVILPGLAD ADAYKRLRDA
VSIPIMAVVV PGTPWFAPTL DELAQIGVEV AIYPAAIMWR VVVAMQEGLA AIRDSNGAPP
ANFDPRIIGQ YLRTADWTQV DSNYA
//
