ID F6GDC7_LACS5 Unreviewed; 478 AA.
AC F6GDC7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:AEH00440.1};
GN OrderedLocusNames=Lacal_0590 {ECO:0000313|EMBL:AEH00440.1};
OS Lacinutrix sp. (strain 5H-3-7-4).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lacinutrix.
OX NCBI_TaxID=983544 {ECO:0000313|EMBL:AEH00440.1, ECO:0000313|Proteomes:UP000008297};
RN [1] {ECO:0000313|EMBL:AEH00440.1, ECO:0000313|Proteomes:UP000008297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5H-3-7-4 {ECO:0000313|EMBL:AEH00440.1,
RC ECO:0000313|Proteomes:UP000008297};
RX PubMed=21725025; DOI=10.1128/JB.05518-11;
RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M.,
RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T.,
RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., Antranikian G.;
RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and
RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of the
RT family Flavobacteriaceae.";
RL J. Bacteriol. 193:4545-4546(2011).
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DR EMBL; CP002825; AEH00440.1; -; Genomic_DNA.
DR AlphaFoldDB; F6GDC7; -.
DR STRING; 983544.Lacal_0590; -.
DR KEGG; lan:Lacal_0590; -.
DR eggNOG; COG1228; Bacteria.
DR HOGENOM; CLU_023620_4_1_10; -.
DR OrthoDB; 9797498at2; -.
DR Proteomes; UP000008297; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 1.20.58.520; Amidohydrolase; 1.
DR Gene3D; 3.30.110.90; Amidohydrolase; 1.
DR Gene3D; 3.40.50.10910; Amidohydrolase; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AEH00440.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008297};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 341..443
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 478 AA; 54455 MW; 736BF3F27B28A11B CRC64;
MKTVKRILKF ILVIIGALLV FIAVMLLVDK QSTNYLNSKN IKSANNNSFL ITNVNIIPMN
QDTVLVNKMV YIKDGIIQKI GNKIETNGVE TLDAKNKYLT PGLIDMHVHV WDRYELGLYL
SNGVTAVRNL WGMPMHLRIK EEANNNEIIS PIFFTTGPKL TGPEFIGDDN LNLNNPHEAK
EKVISFKKRG YDFIKTYYGL DKEIFDAVIE QAKVSNIDIV AHPSQKVPYS YHFNSQIKSI
EHVEEIIQQP LNYNLLDTLK LKEVVNDFSK SKHSAFSPTL TVYNNIYQML INDNILELEQ
LQFMNPLIKR IDSKAQFDRW HSTKLRDSSI IKAIKNQHDL HIKIIKKLHK EGVTFICGTD
AGIGVTIPGF SIHQELAFYK EAGLSNYEVL KTATINASKT HSIMNNMGTI EVGKIANLLL
TDSNPLLELS TLKNPSTIFI KGRKLNKDSL ENFEEKARNR KNLIASAVRY LEHLIFEK
//
