ID A5FBY9_FLAJ1 Unreviewed; 595 AA.
AC A5FBY9;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:ABQ07282.1};
GN OrderedLocusNames=Fjoh_4274 {ECO:0000313|EMBL:ABQ07282.1};
OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ07282.1, ECO:0000313|Proteomes:UP000006694};
RN [1] {ECO:0000313|EMBL:ABQ07282.1, ECO:0000313|Proteomes:UP000006694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC UW101 {ECO:0000313|Proteomes:UP000006694};
RX PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA Cheng Y.Q., Stein J.L.;
RT "Novel features of the polysaccharide-digesting gliding bacterium
RT Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL Appl. Environ. Microbiol. 75:6864-6875(2009).
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DR EMBL; CP000685; ABQ07282.1; -; Genomic_DNA.
DR RefSeq; WP_012026248.1; NZ_MUGZ01000031.1.
DR AlphaFoldDB; A5FBY9; -.
DR STRING; 376686.Fjoh_4274; -.
DR KEGG; fjo:Fjoh_4274; -.
DR eggNOG; COG1574; Bacteria.
DR HOGENOM; CLU_009942_4_3_10; -.
DR OrthoDB; 9767366at2; -.
DR Proteomes; UP000006694; Chromosome.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..595
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030164214"
FT DOMAIN 73..564
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 595 AA; 66609 MW; BEDFEF44A68B502F CRC64;
MKLSFKIAAF LLIISLPIFG QSKKATLIVH HAVIHTLDNK NTIVEAMAVA DGRILKTGKN
SEILKLKDKK TTLIDAKGKT IIPGIFDSHM HIIRGGRFYN TELRWDGVRS LKRALAMLKE
QAQRTPKGQW VRVVGGWNAY QFEEKRLPTL AEINEATGDV PAFILHLYGH AYLNKAGLET
LKIDANTPNP NAGLIEKDSN GNPTGLLAAE PNAFILYSTL AKLPELTQEE KFNSTKQFMT
EMNRLGVTAI MDAGGGFQNF PDDYGVTNGL CKDSDLTIRM PYYLFAQKAG TELNDYTKWM
QTVEIGEGCD DDHHSDKVEY HVQGAGENLV MSAGDFENFD KPRPELSPAM EGQLKEVLSL
LVKNRWPFRI HATYNESITR FLNVIEDINK ETPLNGLLWF FDHAETVSTE NLKRIKALNG
GIAIQHRMAY QGESFIKRYG KTAAANTVPL KKMFELGIKV GMGTDGTRVA SYNPWVGLYW
LTTGKTLGGL KYMNDENIVD RTTALKLFTY GSAQLINIEK DRGMLTADKL ADFSILSDDY
FTTSEENILN IESKLTVVNG KAVYADNDFR TFVNEKPKAI PDWSPVNYFG GYQKN
//
