(data stored in ACNUC30630 zone)

HOGENOM: HAMAR1_8_PE1354

ID   HAMAR1_8_PE1354                      STANDARD;      PRT;   536 AA.
AC   HAMAR1_8_PE1354; Q5V213;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Anthranilate synthase component 1 2; EC=4.1.3 27;AltName:
DE   Full=Anthranilate synthase component I 2; (HAMAR1_8.PE1354).
GN   Name=trpE2; OrderedLocusNames=rrnAC1518;
OS   HALOARCULA MARISMORTUI ATCC 43049.
OC   Archaea; Euryarchaeota; Halobacteria; Halobacteriales; Halobacteriaceae;
OC   Haloarcula.
OX   NCBI_TaxID=272569;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HAMAR1_8.PE1354.
CC       Haloarcula marismortui ATCC 43049 chromosome chromosome I, complete
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:TRPE2_HALMA
CC   -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate +
CC       pyruvate + L-glutamate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC   -!- SUBUNIT: Tetramer of two components I and two components II (By
CC       similarity).
CC   -!- MISCELLANEOUS: Component I catalyzes the formation of anthranilate
CC       using ammonia rather than glutamine, whereas component II provides
CC       glutamine amidotransferase activity.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I
CC       family.
CC   -!- GENE_FAMILY: HOG000025142 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q5V213; -.
DR   EMBL; AY596297; AAV46439.1; -; Genomic_DNA.
DR   RefSeq; YP_136145.1; NC_006396.1.
DR   ProteinModelPortal; Q5V213; -.
DR   GeneID; 3127581; -.
DR   GenomeReviews; AY596297_GR; rrnAC1518.
DR   KEGG; hma:rrnAC1518; -.
DR   NMPDR; fig|272569.1.peg.1410; -.
DR   OMA; SNPIAGT; -.
DR   ProtClustDB; CLSK511484; -.
DR   BioCyc; HMAR272569:RRNAC1518-MON; -.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:EC.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR019999; Anth_synth_I.
DR   InterPro; IPR006805; Anth_synth_I_N.
DR   InterPro; IPR010116; Anthranilate_synth_I_arc.
DR   InterPro; IPR015890; Chorismate-bd_C.
DR   Gene3D; G3DSA:3.60.120.10; TRPE_1_chor_bd; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; TRPE_1_chor_bd; 1.
DR   TIGRFAMs; TIGR01820; TrpE-arch; 1.
DR   HOGENOMDNA; HAMAR1_8.PE1354; -.
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Tryptophan biosynthesis.
SQ   SEQUENCE   536 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTLDISREEF VEHAKADRPV VVRTAAELDV DVEPLTAYAA LTGRTSDVAA NDYTFLLESA
     EKVASSDPDG AFAPETDDRH ARFSFVGYDP RAVVTVTGDE SEVEAFDDRY ADLVTTDGGD
     VVDDLRAAMP DVALRNFPAM DRQHLEGGLV GFLSYDAVYD LWLDEVGLDR PDSRFPDAQF
     VLTTSTVRFD HVEDTVSLVF TPVVRQGEDA GERYGELVAE AERVEAVLSD LSPLSTGGFR
     REDEVAGPRD EYEDAVERAK EYVLSGDIYQ GVISRTRELY GDVDPLGFYE ALRAVNPSPY
     MYLLGYDDLT IVGASPETLV SVAGDHVVSN PIAGTCPRGN SPVEDRRLAG EMLADGKERA
     EHTMLVDLAR NDVRRVAEAG SVRVPEFMNV LKYSHVQHIE STVTGRLAED KDAFDAARAT
     FPAGTLSGAP KIRAMEIIDE LERSPRGPYG GGVGYFDWDG DTDFAIVIRS ATVEDEGDRD
     RITVQAGAGI VADSDPESEY VETEQKMDGV LTALEEIEGE PVDVAERAAG HEEVTR
//

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