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Database: UniProt
Entry: A0A2N5GAN1_9BACI
LinkDB: A0A2N5GAN1_9BACI
Original site: A0A2N5GAN1_9BACI 
ID   A0A2N5GAN1_9BACI        Unreviewed;       536 AA.
AC   A0A2N5GAN1;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:PLR77815.1};
GN   ORFNames=CU633_09140 {ECO:0000313|EMBL:PLR77815.1};
OS   Bacillus sp. V3-13.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2053728 {ECO:0000313|EMBL:PLR77815.1, ECO:0000313|Proteomes:UP000234805};
RN   [1] {ECO:0000313|EMBL:PLR77815.1, ECO:0000313|Proteomes:UP000234805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V3-13 {ECO:0000313|EMBL:PLR77815.1,
RC   ECO:0000313|Proteomes:UP000234805};
RA   Seuylemezian A., Cooper K., Vaishampayan P.;
RT   "Comparitive Functional Genomics of Dry Heat Resistant strains isolated
RT   from the Viking Spacecraft.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:PLR77815.1}.
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DR   EMBL; PGUZ01000022; PLR77815.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5GAN1; -.
DR   OrthoDB; 9767366at2; -.
DR   Proteomes; UP000234805; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01300; YtcJ_like; 1.
DR   Gene3D; 3.10.310.70; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR033932; YtcJ-like.
DR   PANTHER; PTHR22642:SF23; AMIDOHYDROLASE YTCJ-RELATED; 1.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR   Pfam; PF07969; Amidohydro_3; 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:PLR77815.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234805}.
FT   DOMAIN          53..529
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   536 AA;  59218 MW;  365066786B1F9D86 CRC64;
     MGTLWHGGLI YTMETEGEQV EAVYTENGTI IATGTVAGLL EKYQYDISEI NHLHGKTMLP
     GFVDSHMHLI GHGETLIRLD LSRQTSKQAV FKAVKDYADR TAAGKWIIGE GWNENLWENP
     EVISREELDA LVPNHPVLLK RVCRHALVAN SLALKEANIT EATICPPGGV IEKNDSGTLT
     GLLKDQAQDL ILSALPDVDE EYLQTALRAA IKNAWRLGLT GAHTEDLNYY GGFQKTYETF
     KHVIEDEGLR FRAHLLVHHE VAADLYKAGG AFLGGNQWIE FGAIKIFADG ALGGRTALLS
     HPYADDPETS GVAIFTEQQL LDIVKNAREH EMPVAIHTIG DLAFEYALNA LEKSPLQSRG
     RDRLIHAQIL RNDLIGRAKK LPLILDIQPR FTASDFPWVV ERIGEEHMQY CYAWKTLLDA
     GIPCAGGSDA PIEPADPLLG IHAAVTRTNV DDPAKIEYKT EEALSVYEAV SLFTKGSAYA
     ICHEHDRGLI KEGYTADFTV LSENIFQIDP HQIAGIKVMM TVIDGKIVYN VEKPEA
//
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