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Database: UniProt
Entry: Q1DCD0_MYXXD
LinkDB: Q1DCD0_MYXXD
Original site: Q1DCD0_MYXXD 
ID   Q1DCD0_MYXXD            Unreviewed;       387 AA.
AC   Q1DCD0;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=Hydrolase, alpha/beta fold family {ECO:0000313|EMBL:ABF91027.1};
GN   OrderedLocusNames=MXAN_1436 {ECO:0000313|EMBL:ABF91027.1};
OS   Myxococcus xanthus (strain DK1622).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF91027.1, ECO:0000313|Proteomes:UP000002402};
RN   [1] {ECO:0000313|EMBL:ABF91027.1, ECO:0000313|Proteomes:UP000002402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX   PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA   Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA   Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA   Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA   Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA   Kaplan H.B.;
RT   "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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DR   EMBL; CP000113; ABF91027.1; -; Genomic_DNA.
DR   RefSeq; WP_011551552.1; NC_008095.1.
DR   AlphaFoldDB; Q1DCD0; -.
DR   STRING; 246197.MXAN_1436; -.
DR   ESTHER; myxxd-q1dcd0; Abhydr_predicted.
DR   EnsemblBacteria; ABF91027; ABF91027; MXAN_1436.
DR   GeneID; 41358882; -.
DR   KEGG; mxa:MXAN_1436; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_020280_0_0_7; -.
DR   OrthoDB; 5490537at2; -.
DR   Proteomes; UP000002402; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; 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; PTHR11005:SF100; LIPASE-RELATED; 1.
DR   PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ABF91027.1};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          67..327
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   REGION          366..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   387 AA;  43498 MW;  6B38F4B4BDA084DE CRC64;
     MDASRWVVWV LVAGVALVLW NVLWVVAVRR WYRPRAELPQ VLRARCEDGW ELVIHARRAA
     VRRFEEPVLL CHGLAANRFT FDFEPPYSVA HYLTEAGFDC FSVEWRGTGH SRRPPRGRRY
     TDFTIDDHIL QDGPALLELA LKETGAKCAF WLGHSLGGLV GYGVAQGPHG EKLAGLLALG
     APVHFKSEPF LRTLISMGVR AAWPARFRQE WMSASLAPFL GYITLPLSDL LVNPEHIPPR
     IQRQVYANMM SSMSRKVLLQ FQDWIEHDMF RSFDRTKDWR AGIAQLQLPL LVMGGSSDRL
     ATPGNVESQF ALATAPDRTL HIFGTDHGDK MNYGHGDLIF GTGAPSEVYP VIREWLERHA
     SALPAAITDP APAPVEEEPR EPERSVP
//
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