ID D9VZ12_9ACTN Unreviewed; 353 AA.
AC D9VZ12;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Allantoate amidohydrolase {ECO:0000313|EMBL:EFL15555.1};
GN ORFNames=SSNG_02807 {ECO:0000313|EMBL:EFL15555.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL15555.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL15555.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL15555.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., 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 Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M20 family.
CC {ECO:0000256|ARBA:ARBA00006153}.
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DR EMBL; GG657750; EFL15555.1; -; Genomic_DNA.
DR AlphaFoldDB; D9VZ12; -.
DR STRING; 253839.SSNG_02807; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_785060_0_0_11; -.
DR Proteomes; UP000005763; Unassembled WGS sequence.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR NCBIfam; TIGR01879; hydantase; 1.
DR PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EFL15555.1}.
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 36393 MW; 584CBAB703911DAF CRC64;
MTEGSARTGG SAPDPRGSAP GGPATGPRGA AGRPAGAGGA APGASFHTMW AELAPIGRHA
DSGGYRRYAW TGADADCRAW FRAQAESRGL AYEVDRNGNQ WAWLGDPLAG DAVVTGSHLD
SVPDGGAFDG PLGVVSSFAA LDELRARGAA LTRPLAITNF GDEEGARFGL ACVGSRLAAG
QLTKEKAYAL RDADGVSLPQ AMEAAGYDPD SVGADPERLS RIGAFVELHV EQGRALDLSG
DRVGIASAIW PHGRWRFDFH GEANHAGTTR LVDRRDPMLT YAETVLAARR EAALAGAVAT
FGKISVEPNG VNAIPSLVRG WLDSRAADQA NLDTVVTAVE GPPASTPTAT AST
//
