ID S4MPW3_9ACTN Unreviewed; 400 AA.
AC S4MPW3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative N-carbamoyl-L-amino acid hydrolase {ECO:0000313|EMBL:EPJ37615.1};
GN ORFNames=STAFG_5341 {ECO:0000313|EMBL:EPJ37615.1};
OS Streptomyces afghaniensis 772.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1283301 {ECO:0000313|EMBL:EPJ37615.1, ECO:0000313|Proteomes:UP000015001};
RN [1] {ECO:0000313|EMBL:EPJ37615.1, ECO:0000313|Proteomes:UP000015001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=772 {ECO:0000313|EMBL:EPJ37615.1,
RC ECO:0000313|Proteomes:UP000015001};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Fiedler H.-P.,
RA Goodfellow M., Mueller M.;
RT "Draft Genome Sequence of Streptomyces afghaniensis, Which Produces
RT Compounds of the Julimycin B-Complex.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001235-1};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR001235-
CC 1};
CC -!- SIMILARITY: Belongs to the peptidase M20 family.
CC {ECO:0000256|ARBA:ARBA00006153}.
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:EPJ37615.1}.
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DR EMBL; AOPY01001491; EPJ37615.1; -; Genomic_DNA.
DR AlphaFoldDB; S4MPW3; -.
DR PATRIC; fig|1283301.3.peg.5306; -.
DR HOGENOM; CLU_024588_6_0_11; -.
DR Proteomes; UP000015001; Unassembled WGS sequence.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03884; M20_bAS; 1.
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 PIRSF; PIRSF001235; Amidase_carbamoylase; 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:EPJ37615.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015001};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 206
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 264
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 277
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 400 AA; 42217 MW; 8596E4B95C5691EB CRC64;
MWAELLPVGR SSASGGYRRF AWTDADSDCR AWFEEQARSR GLAYEVDRNG NQWAWLGDPA
VGDAVVTGSH LDSVPDGGAF DGPLGVVSAF AALDELRGRD ARFTRPLGIV NFGDEEGARF
GLACVGSRLT AGQLTREQAH RLTDGEGVTL PRAMEAAGYD PDAIGPDPER LARIGAFVEL
HVEQGRALDL SGDRVGIASA IWPHGRWRFD FRGEANHAGT TRLADRRDPM QSYAETVLAA
RREAELAGAV ATFGKIAVEP NGVNAIPSLV RGWLDSRAAD QDSLDAVVAG VEKAAGEYAA
AHGVDLAVVR ESFTPVVEFD HALRDELARI LGKDTGLTVP VLGTGAGHDA GILSGSIPTA
MLFVRNPTGV SHSPAESAAE DDCVAGVLAL ADVLEGLACR
//
