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Database: UniProt
Entry: D7H609_BRUAO
LinkDB: D7H609_BRUAO
Original site: D7H609_BRUAO 
ID   D7H609_BRUAO            Unreviewed;       583 AA.
AC   D7H609;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:EFH32419.1};
GN   ORFNames=BAYG_01923 {ECO:0000313|EMBL:EFH32419.1};
OS   Brucella abortus bv. 5 str. B3196.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=520453 {ECO:0000313|EMBL:EFH32419.1, ECO:0000313|Proteomes:UP000005752};
RN   [1] {ECO:0000313|EMBL:EFH32419.1, ECO:0000313|Proteomes:UP000005752}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B3196 {ECO:0000313|EMBL:EFH32419.1,
RC   ECO:0000313|Proteomes:UP000005752};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Ward D., Whatmore A.M., Perrett L.L., O'Callaghan D., Young S., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Brucella abortus bv. 5 str. B3196.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG774528; EFH32419.1; -; Genomic_DNA.
DR   RefSeq; WP_002968920.1; NZ_GG774528.1.
DR   AlphaFoldDB; D7H609; -.
DR   HOGENOM; CLU_009942_6_1_5; -.
DR   Proteomes; UP000005752; 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:SF25; EXOENZYMES REGULATORY PROTEIN; 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:EFH32419.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..583
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003096977"
FT   DOMAIN          76..580
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   583 AA;  63514 MW;  B079298380D74BF5 CRC64;
     MLYRKLIFLI IIAFSASLST QSAIAESIER ILFNGRIFTA NSEQPLAQAM AIKDGYIFAV
     GSNEEILTYK TANTKLLDLQ NKWGLPGLID AHSHAIIGAL AELSPNLQDE VVDLATLKQR
     IEGWFKQSGH GSGQPFVLFG ANPALWSDPQ ILADIFNKNR WKTQPLLLMG SDLHTAWANG
     AMLHIAGIDD AYVQNLSDHQ RHIIGVTSKG SPDGVLIDAG VDLVTVHLPK PDDEMLLKAG
     QYAVHMNNSY GITGWMDPAA NAGPGEALFS RKPASLGTGI LPAYKLLAEK GQLTAHVAAL
     LVASPLSDAA DLERLDTVRQ QFAAVPNLTM PGIKIFADGV LEFPAQSAAL LGHYKNSGKQ
     GEMLLTAEGL KNLVDAADEK GMLVHIHALG DRAVKQSLDA FEIARKKRNS GISHSITHLQ
     LVDPNDYPRF AALNIMPVMQ LHWAEMDNYL LDLVKPFINE TDFWGQYPAR SLQKNGAVIA
     GASDWPISTA NPWEAMHHAM TREGPDGGLN KAERLDLNTM LLAYTIHAAK AAGIDDKAGS
     LTKGKQADFI IVDRDIFNVS YDLFKNTKVL QTYFAGKLVY SLN
//
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