ID F0SJW2_RUBBR Unreviewed; 429 AA.
AC F0SJW2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=3-dehydroquinate synthase {ECO:0000313|EMBL:ADY58651.1};
DE EC=4.2.3.4 {ECO:0000313|EMBL:ADY58651.1};
GN OrderedLocusNames=Plabr_1030 {ECO:0000313|EMBL:ADY58651.1};
OS Rubinisphaera brasiliensis (strain ATCC 49424 / DSM 5305 / JCM 21570 / IAM
OS 15109 / NBRC 103401 / IFAM 1448) (Planctomyces brasiliensis).
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae; Rubinisphaera.
OX NCBI_TaxID=756272 {ECO:0000313|EMBL:ADY58651.1, ECO:0000313|Proteomes:UP000006860};
RN [1] {ECO:0000313|Proteomes:UP000006860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448
RC {ECO:0000313|Proteomes:UP000006860};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Lu M.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Planctomyces brasiliensis DSM 5305.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911};
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DR EMBL; CP002546; ADY58651.1; -; Genomic_DNA.
DR RefSeq; WP_013627386.1; NC_015174.1.
DR AlphaFoldDB; F0SJW2; -.
DR STRING; 756272.Plabr_1030; -.
DR KEGG; pbs:Plabr_1030; -.
DR eggNOG; COG0337; Bacteria.
DR HOGENOM; CLU_001201_0_4_0; -.
DR Proteomes; UP000006860; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd08198; DHQS-like; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR030960; DHQS/DOIS.
DR PANTHER; PTHR43622; 3-DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR43622:SF7; 3-DEHYDROQUINATE SYNTHASE, CHLOROPLASTIC; 1.
DR Pfam; PF01761; DHQ_synthase; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ADY58651.1};
KW Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000006860};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 130..379
FT /note="3-dehydroquinate synthase"
FT /evidence="ECO:0000259|Pfam:PF01761"
FT REGION 18..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 47685 MW; 1AE0F079C979D0D9 CRC64;
MLRRAVWSGV SPSIDGLQSS ERCLAAESDP EISKQPDAMK QTTTQPATAQ RLDIQFQVPM
THRLRFTQDV LGDQFSELLA LLETSDDKPA RVQFWLDETL LSARPDLKQQ LRDRVAEHPQ
QVQLASNVQV VPGGEAVKND VHILERMLKV MNAADLDRRS YVIVIGGGAV LDAVGFAAAI
AHRGIRLIRL PTTTLGQADS GVGVKNSINL FHKKNWVGTF ATPWAVINDA ELLETLPDRD
FRAGFSEAVK VALLKETELF EFIHANAAKI QDREWSVCEP VIRRSAEWHI RHITQGGDPF
EALEARPLDF GHWSAHKLEV MSDFELRHGE AVAIGLAIDV LYSKRKLGLS AERADQVLDC
LRQMGILLSH PTLLEVDTLF GGLEEFRQHL GGRLTLTMLT DVGKPLEIHE VDDAAMRDSI
RELIATVSA
//
