PHZF_PSEFL
ID PHZF_PSEFL Reviewed; 278 AA.
AC Q51792;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Trans-2,3-dihydro-3-hydroxyanthranilate isomerase;
DE EC=5.3.3.17 {ECO:0000269|PubMed:15449932, ECO:0000269|PubMed:15545603, ECO:0000269|PubMed:19053436};
DE AltName: Full=Phenazine/pyocyanine biosynthesis protein PhzF;
GN Name=phzF;
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NRRL B-15132 / 2-79;
RX PubMed=9573209; DOI=10.1128/jb.180.9.2541-2548.1998;
RA Mavrodi D.V., Ksenzenko V.N., Bonsall R.F., Cook R.J., Boronin A.M.,
RA Thomashow L.S.;
RT "A seven-gene locus for synthesis of phenazine-1-carboxylic acid by
RT Pseudomonas fluorescens 2-79.";
RL J. Bacteriol. 180:2541-2548(1998).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19053436; DOI=10.1021/ja806325k;
RA Ahuja E.G., Janning P., Mentel M., Graebsch A., Breinbauer R., Hiller W.,
RA Costisella B., Thomashow L.S., Mavrodi D.V., Blankenfeldt W.;
RT "PhzA/B catalyzes the formation of the tricycle in phenazine
RT biosynthesis.";
RL J. Am. Chem. Soc. 130:17053-17061(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=NRRL B-15132 / 2-79;
RX PubMed=15449932; DOI=10.1021/bi049059z;
RA Parsons J.F., Song F., Parsons L., Calabrese K., Eisenstein E.,
RA Ladner J.E.;
RT "Structure and function of the phenazine biosynthesis protein PhzF from
RT Pseudomonas fluorescens 2-79.";
RL Biochemistry 43:12427-12435(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RX PubMed=15545603; DOI=10.1073/pnas.0407371101;
RA Blankenfeldt W., Kuzin A.P., Skarina T., Korniyenko Y., Tong L., Bayer P.,
RA Janning P., Thomashow L.S., Mavrodi D.V.;
RT "Structure and function of the phenazine biosynthetic protein PhzF from
RT Pseudomonas fluorescens.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16431-16436(2004).
CC -!- FUNCTION: Isomerase that catalyzes the condensation of two molecules of
CC trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) into the phenazine
CC ring system. The final product is not yet known.
CC {ECO:0000269|PubMed:15545603, ECO:0000269|PubMed:19053436}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S,6S)-6-amino-5-hydroxycyclohexa-1,3-diene-1-carboxyate =
CC (1R,6S)-6-amino-5-oxocyclohex-2-ene-1-carboxylate;
CC Xref=Rhea:RHEA:28182, ChEBI:CHEBI:60849, ChEBI:CHEBI:60862;
CC EC=5.3.3.17; Evidence={ECO:0000269|PubMed:15449932,
CC ECO:0000269|PubMed:15545603, ECO:0000269|PubMed:19053436};
CC -!- PATHWAY: Antibiotic biosynthesis; phenazine biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15449932,
CC ECO:0000269|PubMed:15545603}.
CC -!- SIMILARITY: Belongs to the PhzF family. {ECO:0000305}.
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DR EMBL; L48616; AAC18905.1; -; Genomic_DNA.
DR RefSeq; WP_043050175.1; NZ_JXCQ01000041.1.
DR PDB; 1T6K; X-ray; 1.80 A; A=1-278.
DR PDB; 1U1V; X-ray; 1.70 A; A=1-278.
DR PDB; 1U1W; X-ray; 1.35 A; A/B=1-278.
DR PDB; 1U1X; X-ray; 1.88 A; A/B=1-278.
DR PDB; 1XUA; X-ray; 1.90 A; A/B=1-278.
DR PDB; 1XUB; X-ray; 1.30 A; A=1-278.
DR PDB; 5IWE; X-ray; 1.71 A; A=1-278.
DR PDBsum; 1T6K; -.
DR PDBsum; 1U1V; -.
DR PDBsum; 1U1W; -.
DR PDBsum; 1U1X; -.
DR PDBsum; 1XUA; -.
DR PDBsum; 1XUB; -.
DR PDBsum; 5IWE; -.
DR AlphaFoldDB; Q51792; -.
DR SMR; Q51792; -.
DR DrugBank; DB02124; (2s,3s)-Trans-2,3-Dihydro-3-Hydroxyanthranilic Acid.
DR DrugBank; DB03644; 3-hydroxyanthranilic acid.
DR KEGG; ag:AAC18905; -.
DR BioCyc; MetaCyc:MON-13700; -.
DR BRENDA; 5.3.3.17; 5121.
DR UniPathway; UPA00099; -.
DR EvolutionaryTrace; Q51792; -.
DR GO; GO:0102943; F:trans-2,3-dihydro-3-hydroxy-anthranilate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0002047; P:phenazine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR003719; Phenazine_PhzF.
DR PANTHER; PTHR13774; PTHR13774; 1.
DR Pfam; PF02567; PhzC-PhzF; 1.
DR PIRSF; PIRSF016184; PhzC_PhzF; 1.
DR TIGRFAMs; TIGR00654; PhzF_family; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Isomerase; Virulence.
FT CHAIN 1..278
FT /note="Trans-2,3-dihydro-3-hydroxyanthranilate isomerase"
FT /id="PRO_0000162382"
FT ACT_SITE 45
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:1XUB"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1XUB"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 53..63
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1XUB"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 99..108
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:1XUB"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 147..159
FT /evidence="ECO:0007829|PDB:1XUB"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:1XUB"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:1XUB"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1XUB"
FT HELIX 212..224
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:1XUB"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:1XUB"
FT STRAND 258..276
FT /evidence="ECO:0007829|PDB:1XUB"
SQ SEQUENCE 278 AA; 30053 MW; 345086CE9679224D CRC64;
MHNYVIIDAF ASVPLEGNPV AVFFDADDLP PAQMQRIARE MNLSESTFVL KPRNGGDALI
RIFTPVNELP FAGHPLLGTA IALGAHTDNH RLYLETQMGT IAFELERQNG SVIAASMDQP
IPTWTALGRD AELLKALGIS DSTFPIEIYH NGPRHVFVGL PSIDALSALH PDHRALSNFH
DMAINCFAGA GRRWRSRMFS PAYGVVEDAA TGSAAGPLAI HLARHGQIEF GQPVEILQGV
EIGRPSLMFA KAEGRAEQLT RVEVSGNGVT FGRGTIVL
