ID A0A132ML96_9ACTN Unreviewed; 349 AA.
AC A0A132ML96;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Cyclohexadienyl dehydratase {ECO:0000313|EMBL:KWW98563.1};
DE EC=4.2.1.51 {ECO:0000313|EMBL:KWW98563.1};
GN ORFNames=LI90_189 {ECO:0000313|EMBL:KWW98563.1};
OS Carbonactinospora thermoautotrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Carbonactinosporaceae; Carbonactinospora.
OX NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWW98563.1, ECO:0000313|Proteomes:UP000070188};
RN [1] {ECO:0000313|Proteomes:UP000070188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|Proteomes:UP000070188};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Chang R., Ford T., Nguyen P.Q., Woodward J., Permingeat H., Joshi N.S.,
RA Silver P.A., Usadel B., Rutherford A.W., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000256|ARBA:ARBA00010333, ECO:0000256|RuleBase:RU003744}.
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:KWW98563.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LAXD01000001; KWW98563.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132ML96; -.
DR STRING; 1469144.LI90_189; -.
DR PATRIC; fig|1469144.10.peg.263; -.
DR Proteomes; UP000070188; Unassembled WGS sequence.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
DR CDD; cd01069; PBP2_PheC; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR037298; PheC_PBP2.
DR InterPro; IPR018313; SBP_3_CS.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR PANTHER; PTHR35936:SF19; ABC TRANSPORTER ARGININE-BINDING PROTEIN ARTJ-RELATED; 1.
DR PANTHER; PTHR35936; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F; 1.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00062; PBPb; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:KWW98563.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070188};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 126..349
FT /note="Solute-binding protein family 3/N-terminal"
FT /evidence="ECO:0000259|SMART:SM00062"
FT REGION 36..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 38869 MW; 1A9E474304A0552C CRC64;
MRGRSYTAWL GAALPGELGR RGLAVPVADL AERSAGDLGF GRRPPPRHGV RAEAARCRRA
RRHDRQRSSL RQNLDQQSYP EESPMKLAAS LAALTLALLT GGTAVVAGHR TPAHQTALEE
VVERGEIRVC TTGDYRPFTY RDPKTGQYTG IDVDMAKDLA AALGVRVTFV PTTWRTLMSD
FTAGRCDIGA GGVSVTLDRA RQAYFSEPYL RDGKTPITRC ENASRFQTLA QIDQPGVRVV
VNPGGTNERF ARENLKQATI VVHEDNTTIF DQIVAGRADL MITDSSEARY QAKIHPELCA
VHPDQPFTFA EKAYLLPRGD EEFKHWVDQW VHLRTHDGTY RRLSDAWMR
//
