ID N9GT77_ACIHA Unreviewed; 579 AA.
AC N9GT77;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN ORFNames=F927_00935 {ECO:0000313|EMBL:ENW20451.1};
OS Acinetobacter haemolyticus CIP 64.3 = MTCC 9819.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217659 {ECO:0000313|EMBL:ENW20451.1, ECO:0000313|Proteomes:UP000017667};
RN [1] {ECO:0000313|EMBL:ENW20451.1, ECO:0000313|Proteomes:UP000017667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 64.3 {ECO:0000313|EMBL:ENW20451.1,
RC ECO:0000313|Proteomes:UP000017667};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter haemolyticus CIP 64.3.";
RL Submitted (FEB-2013) 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:ENW20451.1}.
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DR EMBL; APQQ01000012; ENW20451.1; -; Genomic_DNA.
DR RefSeq; WP_005087345.1; NZ_KB849812.1.
DR AlphaFoldDB; N9GT77; -.
DR PATRIC; fig|1217659.3.peg.915; -.
DR HOGENOM; CLU_009942_2_1_6; -.
DR Proteomes; UP000017667; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..579
FT /note="Amidohydrolase 3 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004143011"
FT DOMAIN 81..574
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 579 AA; 64334 MW; 30CFB7C7185672D5 CRC64;
MTFKNLNKLT LATIIGLALS GCVTTPNETV SAEKLFYGGP ILTMEGMTPE YVEALLVKDG
KIVYAGPKKQ AESLIEARAQ YIDLKNRTLL PSFIDAHSHV NMVGFHQMVA NLYPAPDGQV
SDIDSLVQVL TQWKKQNPQV IETMGGWILG NGYDDAQLSE QRHPTATDLD RVSKDQPVMV
LHQSGHLASV NHKALALLKI DQNTTNPAGG VIRREANSNV PNGVLEESAL FTAIGSIFKD
VPAEVMFEIA RKGLDAYVKN GFTTVQEGRA DQGTTEMWQA LAKQNQLPID VVSYPDITTS
QDYMLKQGSS RQYDQHFRIG GVKISLDGSP QGKTAWLTQA YVIPPEGKDQ NYKGYPAIKD
DQQVNQYINL AFEQGWQVLA HANGDAAIDQ FIGAVKDATA KQGKADRRSA LIHSQTIRDD
QLDQLKALDI IPSFFSLHTY YWGDWHRQQT LGETRAAHIS PTATALKKNL IFTEHHDAPV
VPPHSMMMID ATVNRLTRTN YVLGKNERVS PYFALKSITD WAAYQYFEEQ TKGTLTKGKL
ADLVILEHNP LTVPNRNIKD IQILATYKEG QLIYTNSKN
//
