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FBIA_MYCS2
ID   FBIA_MYCS2              Reviewed;         327 AA.
AC   A0QTG2; I7G6J5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Phosphoenolpyruvate transferase {ECO:0000255|HAMAP-Rule:MF_01257};
DE            EC=2.7.8.28 {ECO:0000255|HAMAP-Rule:MF_01257};
DE   AltName: Full=EPPG:FO PEP transferase {ECO:0000255|HAMAP-Rule:MF_01257};
GN   Name=fbiA {ECO:0000255|HAMAP-Rule:MF_01257};
GN   OrderedLocusNames=MSMEG_1830, MSMEI_1787;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
CC   -!- FUNCTION: Catalyzes the transfer of the phosphoenolpyruvate moiety from
CC       enoylpyruvoyl-2-diphospho-5'-guanosine (EPPG) to 7,8-didemethyl-8-
CC       hydroxy-5-deazariboflavin (FO) with the formation of dehydro coenzyme
CC       F420-0 and GMP. {ECO:0000255|HAMAP-Rule:MF_01257}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,8-didemethyl-8-hydroxy-5-deazariboflavin + enolpyruvoyl-2-
CC         diphospho-5'-guanosine = dehydro coenzyme F420-0 + GMP + H(+);
CC         Xref=Rhea:RHEA:27510, ChEBI:CHEBI:15378, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:59904, ChEBI:CHEBI:143701, ChEBI:CHEBI:143705;
CC         EC=2.7.8.28; Evidence={ECO:0000255|HAMAP-Rule:MF_01257};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01257};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01257}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01257}.
CC   -!- SIMILARITY: Belongs to the CofD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01257}.
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DR   EMBL; CP000480; ABK71517.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP38259.1; -; Genomic_DNA.
DR   RefSeq; WP_011727938.1; NZ_SIJM01000028.1.
DR   RefSeq; YP_886200.1; NC_008596.1.
DR   PDB; 6UVX; X-ray; 2.30 A; A/B=1-327.
DR   PDB; 6UW1; X-ray; 2.21 A; A/B=1-327.
DR   PDB; 6UW3; X-ray; 2.40 A; A/B=1-327.
DR   PDB; 6UW5; X-ray; 2.20 A; A/B=1-327.
DR   PDB; 6UW7; X-ray; 2.34 A; A/B=1-327.
DR   PDBsum; 6UVX; -.
DR   PDBsum; 6UW1; -.
DR   PDBsum; 6UW3; -.
DR   PDBsum; 6UW5; -.
DR   PDBsum; 6UW7; -.
DR   AlphaFoldDB; A0QTG2; -.
DR   SMR; A0QTG2; -.
DR   STRING; 246196.MSMEI_1787; -.
DR   EnsemblBacteria; ABK71517; ABK71517; MSMEG_1830.
DR   EnsemblBacteria; AFP38259; AFP38259; MSMEI_1787.
DR   GeneID; 66733267; -.
DR   KEGG; msg:MSMEI_1787; -.
DR   KEGG; msm:MSMEG_1830; -.
DR   PATRIC; fig|246196.19.peg.1812; -.
DR   eggNOG; COG0391; Bacteria.
DR   OMA; DLDTVMY; -.
DR   OrthoDB; 1079756at2; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0043743; F:LPPG:FO 2-phospho-L-lactate transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   CDD; cd07186; CofD_like; 1.
DR   Gene3D; 3.40.50.10680; -; 1.
DR   HAMAP; MF_01257; CofD; 1.
DR   InterPro; IPR002882; CofD.
DR   InterPro; IPR038136; CofD-like_dom_sf.
DR   InterPro; IPR010115; FbiA/CofD.
DR   PANTHER; PTHR43007; PTHR43007; 1.
DR   Pfam; PF01933; CofD; 1.
DR   SUPFAM; SSF142338; SSF142338; 1.
DR   TIGRFAMs; TIGR01819; F420_cofD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Magnesium; Reference proteome; Transferase.
FT   CHAIN           1..327
FT                   /note="Phosphoenolpyruvate transferase"
FT                   /id="PRO_1000067251"
FT   BINDING         59
FT                   /ligand="7,8-didemethyl-8-hydroxy-5-deazariboflavin"
FT                   /ligand_id="ChEBI:CHEBI:59904"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01257"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   HELIX           10..23
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   STRAND          36..41
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   HELIX           56..65
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   TURN            71..73
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   STRAND          74..77
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   HELIX           83..90
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   HELIX           102..116
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   HELIX           121..132
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   STRAND          135..141
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   STRAND          147..153
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   TURN            155..157
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   STRAND          160..164
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   HELIX           165..169
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   STRAND          178..184
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   HELIX           186..188
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   HELIX           195..200
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   STRAND          203..207
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   TURN            212..215
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   HELIX           216..220
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   HELIX           223..231
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   STRAND          236..239
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   STRAND          249..251
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   HELIX           252..258
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   HELIX           265..272
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   TURN            275..278
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   STRAND          281..287
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   STRAND          298..302
FT                   /evidence="ECO:0007829|PDB:6UW5"
FT   HELIX           309..323
FT                   /evidence="ECO:0007829|PDB:6UW5"
SQ   SEQUENCE   327 AA;  34754 MW;  061F4C7BE305ACC2 CRC64;
     MKITVLVGGV GGARFLLGVQ NLLGLGSFAD GPSKHELTAV VNIGDDAWMH GVRICPDLDT
     CMYTLGGGID PDRGWGHRNE TWNAKEELAA YGVQPDWFGL GDRDLATHLV RSQMLRAGYP
     LSQVTEALCK RWQPGARLLP ASDERSETHV VITDPTDGER RAIHFQEWWV RYRAKVPTHS
     FAYVGADQAT AGPGVVEAIG DADIVLLAPS NPVVSIGPIL QIPGIRGALR STSAPVIGYS
     PIIAGKPLRG MADECLKVIG VESTSQAVGE FFGARAGTGL LDGWLVHEGD HAQIEGVKVK
     AVPLLMTDPE ATAAMVRAGL DLAGVSL
 
 
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