ID Q2G9T7_NOVAD Unreviewed; 284 AA.
AC Q2G9T7;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Alpha/beta hydrolase {ECO:0000313|EMBL:ABD25386.1};
GN OrderedLocusNames=Saro_0941 {ECO:0000313|EMBL:ABD25386.1};
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238 {ECO:0000313|EMBL:ABD25386.1, ECO:0000313|Proteomes:UP000009134};
RN [1] {ECO:0000313|Proteomes:UP000009134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC / F199 {ECO:0000313|Proteomes:UP000009134};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:3BWX}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH CA(2+).
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of an alpha/beta hydrolase (YP_496220.1) from
RT Novosphingobium aromaticivorans DSM 12444 at 1.50 A resolution.";
RL Submitted (JAN-2008) to the PDB data bank.
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DR EMBL; CP000248; ABD25386.1; -; Genomic_DNA.
DR RefSeq; WP_011444600.1; NC_007794.1.
DR PDB; 3BWX; X-ray; 1.50 A; A=1-284.
DR PDBsum; 3BWX; -.
DR AlphaFoldDB; Q2G9T7; -.
DR SMR; Q2G9T7; -.
DR STRING; 279238.Saro_0941; -.
DR ESTHER; novad-q2g9t7; 6_AlphaBeta_hydrolase.
DR DNASU; 3918027; -.
DR KEGG; nar:Saro_0941; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_1_1_5; -.
DR EvolutionaryTrace; Q2G9T7; -.
DR Proteomes; UP000009134; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR PANTHER; PTHR43194; HYDROLASE ALPHA/BETA FOLD FAMILY; 1.
DR PANTHER; PTHR43194:SF2; PEROXISOMAL MEMBRANE PROTEIN LPX1; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3BWX}; Calcium {ECO:0007829|PDB:3BWX};
KW Hydrolase {ECO:0000313|EMBL:ABD25386.1};
KW Metal-binding {ECO:0007829|PDB:3BWX};
KW Reference proteome {ECO:0000313|Proteomes:UP000009134}.
FT DOMAIN 31..276
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF12697"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:3BWX"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:3BWX"
SQ SEQUENCE 284 AA; 31440 MW; 6B6CD44DBAB40587 CRC64;
MAEYEDRYWT SSDGLRLHFR AYEGDISRPP VLCLPGLTRN ARDFEDLATR LAGDWRVLCP
EMRGRGDSDY AKDPMTYQPM QYLQDLEALL AQEGIERFVA IGTSLGGLLT MLLAAANPAR
IAAAVLNDVG PEVSPEGLER IRGYVGQGRN FETWMHAARA LQESSGDVYP DWDITQWLRY
AKRIMVLGSS GRIAFDYDMK IAEPFEAPAG ATPQVDMWPL FDALATRPLL VLRGETSDIL
SAQTAAKMAS RPGVELVTLP RIGHAPTLDE PESIAAIGRL LERV
//
