ID A0A1X7ALV4_9GAMM Unreviewed; 433 AA.
AC A0A1X7ALV4;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Indole-3-acetyl-aspartic acid hydrolase {ECO:0000313|EMBL:SMA48757.1};
DE EC=3.5.1.- {ECO:0000313|EMBL:SMA48757.1};
GN Name=iaaH {ECO:0000313|EMBL:SMA48757.1};
GN ORFNames=EHSB41UT_02874 {ECO:0000313|EMBL:SMA48757.1};
OS Parendozoicomonas haliclonae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Parendozoicomonas.
OX NCBI_TaxID=1960125 {ECO:0000313|EMBL:SMA48757.1, ECO:0000313|Proteomes:UP000196573};
RN [1] {ECO:0000313|EMBL:SMA48757.1, ECO:0000313|Proteomes:UP000196573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB41UT1 {ECO:0000313|EMBL:SMA48757.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FWPT01000006; SMA48757.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7ALV4; -.
DR OrthoDB; 9777385at2; -.
DR Proteomes; UP000196573; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR30575:SF3; M20_DIMER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR30575; PEPTIDASE M20; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SMA48757.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000196573}.
FT DOMAIN 235..323
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 433 AA; 46711 MW; 362A3FF14C36E3E1 CRC64;
MQNRVNAFVD SIEADVIAHR RNFHRYPELG WHEIRTASLI ARQLAADGIP FKLGREVFKE
DDRMGLPSQQ EMDANYQRAL VQGADPEYAP LFKDGFTGIV ATIGSGDGPT IALRFDIDAL
PIEESTASDH FPTAQGFASE NQGIMHSCGH DGHAAIGLGV CKTLKHFEEQ LKAPVKIFFQ
PAEEGVRGGK AMASSGELEG IQYLIAGHLS SKEGDNGYLS VKSREILATT KLDAVFTGKS
AHAGAAPQDG KNALLAASTA ILNIHAIPRH AGGYSVANVG KVTAGTMRNG ICSDATLLIE
TRGHSTAIND YLEANTLRIL KAAAEMYDCE LSISYQGSAE SCECDDELAD IARQVALEIP
EYIQVVDNFE MVGSEDATYL MNRVKQQGGK ATYMTYGSLG GMGHHKPHFD IDESDMVLAV
KLFSGMALRI QTS
//