(data stored in SCRATCH zone)

SWISSPROT: A4AT91_MARSH

ID   A4AT91_MARSH            Unreviewed;       330 AA.
AC   A4AT91;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   RecName: Full=Anthranilate phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS01090345};
DE            EC=2.4.2.18 {ECO:0000256|HAMAP-Rule:MF_00211, ECO:0000256|SAAS:SAAS01090347};
GN   Name=trpD {ECO:0000256|HAMAP-Rule:MF_00211};
GN   OrderedLocusNames=FB2170_16291 {ECO:0000313|EMBL:EAR00661.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00661.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00661.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
CC   -!- FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5-
CC       phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield
CC       N-(5'-phosphoribosyl)-anthranilate (PRA). {ECO:0000256|HAMAP-
CC       Rule:MF_00211, ECO:0000256|SAAS:SAAS00918330}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate =
CC         5-phospho-alpha-D-ribose 1-diphosphate + anthranilate;
CC         Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00211,
CC         ECO:0000256|SAAS:SAAS01124167};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00211};
CC       Note=Binds 2 magnesium ions per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00211};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 2/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00211, ECO:0000256|SAAS:SAAS00083106}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00211,
CC       ECO:0000256|SAAS:SAAS00918319}.
CC   -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00211,
CC       ECO:0000256|SAAS:SAAS01090338}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00211}.
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DR   EMBL; CP002157; EAR00661.1; -; Genomic_DNA.
DR   RefSeq; WP_013304464.1; NC_014472.1.
DR   STRING; 313603.FB2170_16291; -.
DR   EnsemblBacteria; EAR00661; EAR00661; FB2170_16291.
DR   KEGG; fbc:FB2170_16291; -.
DR   eggNOG; ENOG4107RI6; Bacteria.
DR   eggNOG; COG0547; LUCA.
DR   HOGENOM; HOG000230451; -.
DR   KO; K00766; -.
DR   OMA; HHSAMKH; -.
DR   OrthoDB; 1238435at2; -.
DR   BioCyc; MSP313603:G1GNS-37-MONOMER; -.
DR   UniPathway; UPA00035; UER00041.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1030.10; -; 1.
DR   HAMAP; MF_00211; TrpD; 1.
DR   InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase.
DR   InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR   InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR   InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom)sf.
DR   InterPro; IPR035902; Nuc_phospho_transferase.
DR   Pfam; PF02885; Glycos_trans_3N; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   SUPFAM; SSF47648; SSF47648; 1.
DR   SUPFAM; SSF52418; SSF52418; 1.
DR   TIGRFAMs; TIGR01245; trpD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4AT91.
DR   SWISS-2DPAGE; A4AT91.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211,
KW   ECO:0000256|SAAS:SAAS00458438};
KW   Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211,
KW   ECO:0000256|SAAS:SAAS00458470};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00211,
KW   ECO:0000256|SAAS:SAAS00083140, ECO:0000313|EMBL:EAR00661.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00211,
KW   ECO:0000256|SAAS:SAAS00918354};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00211,
KW   ECO:0000256|SAAS:SAAS00918356};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00211,
KW   ECO:0000256|SAAS:SAAS00458476, ECO:0000313|EMBL:EAR00661.1};
KW   Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00211,
KW   ECO:0000256|SAAS:SAAS00458450}.
FT   DOMAIN        2     62       Glycos_trans_3N. {ECO:0000259|Pfam:
FT                                PF02885}.
FT   DOMAIN       74    317       Glycos_transf_3. {ECO:0000259|Pfam:
FT                                PF00591}.
FT   REGION       82     83       Phosphoribosylpyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00211}.
FT   REGION       89     92       Phosphoribosylpyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00211}.
FT   REGION      107    115       Phosphoribosylpyrophosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00211}.
FT   METAL        91     91       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00211}.
FT   METAL       223    223       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00211}.
FT   METAL       224    224       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00211}.
FT   METAL       224    224       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00211}.
FT   BINDING      79     79       Anthranilate 1; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00211}.
FT   BINDING      79     79       Phosphoribosylpyrophosphate; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00211}.
FT   BINDING      87     87       Phosphoribosylpyrophosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00211}.
FT   BINDING     110    110       Anthranilate 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00211}.
FT   BINDING     119    119       Phosphoribosylpyrophosphate; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00211}.
FT   BINDING     165    165       Anthranilate 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00211}.
SQ   SEQUENCE   330 AA;  35671 MW;  85194D74302AE34F CRC64;
     MKDILNRLIN HDILTKEDAK QVLVNIAKGE YNTSQIAAFL TVYMMRSITI EELEGFRNAL
     LELCLAIDLS DYNPIDLCGT GGDGKDTFNI STLASFVTAG AGVKVTKHGN YGVSSKCGSS
     NVMEFLGIKF SNEADFLKKS IDEAGICVLH APLFHPAMKN VAPIRRELAV KTFFNMLGPM
     VNPAFPKNQM VGVFNLELAR MYGYLYQNTD KNFTVLHALD GYDEISLTGA TKTISNNSEG
     ILNPEDFGIK GVTQSQIEGG ETIEESAKIF MTILQGKGTE AQNNVVCANA GIAIATVNGL
     NPKEGFEKAK ESLLGGHGLT ALKKLQTLSA
//

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