ID A0A2I0NZM9_9EURY Unreviewed; 193 AA.
AC A0A2I0NZM9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|HAMAP-Rule:MF_00135};
DE Short=PRAI {ECO:0000256|HAMAP-Rule:MF_00135};
DE EC=5.3.1.24 {ECO:0000256|HAMAP-Rule:MF_00135};
GN Name=trpF {ECO:0000256|HAMAP-Rule:MF_00135};
GN ORFNames=CVV33_07855 {ECO:0000313|EMBL:PKL59433.1};
OS Methanomicrobiales archaeon HGW-Methanomicrobiales-4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales.
OX NCBI_TaxID=2013820 {ECO:0000313|EMBL:PKL59433.1, ECO:0000313|Proteomes:UP000233538};
RN [1] {ECO:0000313|EMBL:PKL59433.1, ECO:0000313|Proteomes:UP000233538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGW-Methanomicrobiales-4 {ECO:0000313|EMBL:PKL59433.1};
RX PubMed=28350393; DOI=10.1038/ismej.2017.39;
RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., Anantharaman K.,
RA Probst A., Burstein D., Thomas B.C., Banfield J.F.;
RT "Potential for microbial H2 and metal transformations associated with novel
RT bacteria and archaea in deep terrestrial subsurface sediments.";
RL ISME J. 11:1915-1929(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-
CC carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613;
CC EC=5.3.1.24; Evidence={ECO:0000256|ARBA:ARBA00001164,
CC ECO:0000256|HAMAP-Rule:MF_00135};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5. {ECO:0000256|ARBA:ARBA00004664,
CC ECO:0000256|HAMAP-Rule:MF_00135}.
CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000256|ARBA:ARBA00007571,
CC ECO:0000256|HAMAP-Rule:MF_00135}.
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:PKL59433.1}.
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DR EMBL; PGYJ01000428; PKL59433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0NZM9; -.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000233538; Unassembled WGS sequence.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00405; PRAI; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00135; PRAI; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001240; PRAI_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR044643; TrpF_fam.
DR PANTHER; PTHR42894; N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE; 1.
DR PANTHER; PTHR42894:SF1; N-(5'-PHOSPHORIBOSYL)ANTHRANILATE ISOMERASE; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135};
KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00135, ECO:0000313|EMBL:PKL59433.1};
KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00135}.
FT DOMAIN 4..188
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
SQ SEQUENCE 193 AA; 20823 MW; 7E40B24B51A10AA7 CRC64;
MRVKLCGITR PEDAHLADIT GADAIGVVLF SDSPRSVEPR KAAEIFQAAG PYMGRICVTH
TKSRSDLEEM LDLCPTAIQI SYPHRIPKDR NVQVIRVIEP GMPIPHEGDT DALIVDASQG
KGKTYDPVFV REVMGKTSLP VILAGGLHPG NVAEAIRTIH PYAVDVASGI ETAPGIKDPA
KVRAFVQNSR ILL
//
