Y1171_HAEIN
ID Y1171_HAEIN Reviewed; 193 AA.
AC P44339;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Putative anthranilate synthase component II;
DE EC=4.1.3.27;
DE AltName: Full=Glutamine amido-transferase;
GN OrderedLocusNames=HI_1171;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
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.
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DR EMBL; L42023; AAC22824.1; -; Genomic_DNA.
DR PIR; G64187; G64187.
DR RefSeq; NP_439329.1; NC_000907.1.
DR RefSeq; WP_005694270.1; NC_000907.1.
DR AlphaFoldDB; P44339; -.
DR SMR; P44339; -.
DR STRING; 71421.HI_1171; -.
DR EnsemblBacteria; AAC22824; AAC22824; HI_1171.
DR KEGG; hin:HI_1171; -.
DR PATRIC; fig|71421.8.peg.1223; -.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_014340_1_2_6; -.
DR OMA; FNIGLYH; -.
DR PhylomeDB; P44339; -.
DR BioCyc; HINF71421:G1GJ1-1205-MON; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IBA:GO_Central.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IBA:GO_Central.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Glutamine amidotransferase; Lyase; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..193
FT /note="Putative anthranilate synthase component II"
FT /id="PRO_0000056879"
FT DOMAIN 2..193
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 193 AA; 22300 MW; 2C6468C440E56999 CRC64;
MKLLIINNHD SFTFNLVDLI RKLNVPYDVL NVEDLKENTA ENYSHILISP GPDIPRAYPQ
LFSMLEKYYQ QKSILGVCLG HQTLCEFFGG TLYNLENVRH GQKRTLKVRS NSPLFFDLPT
EFNIGLYHSW GVQEEDFPDC LEITALCDED VVMAMQHKSL PIYSVQFHPE SYMSDFGEKI
LRNWLAIPPT TNP