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Database: UniProt
Entry: A0A1H3FLX8_9EURY
LinkDB: A0A1H3FLX8_9EURY
Original site: A0A1H3FLX8_9EURY 
ID   A0A1H3FLX8_9EURY        Unreviewed;       671 AA.
AC   A0A1H3FLX8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=N-methylhydantoinase A {ECO:0000313|EMBL:SDX91961.1};
GN   ORFNames=SAMN04487946_10445 {ECO:0000313|EMBL:SDX91961.1};
OS   Halobellus clavatus.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Halobellus.
OX   NCBI_TaxID=660517 {ECO:0000313|EMBL:SDX91961.1, ECO:0000313|Proteomes:UP000199170};
RN   [1] {ECO:0000313|Proteomes:UP000199170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10118 {ECO:0000313|Proteomes:UP000199170};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNPB01000004; SDX91961.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3FLX8; -.
DR   STRING; 660517.SAMN04487946_10445; -.
DR   OrthoDB; 8261at2157; -.
DR   Proteomes; UP000199170; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   InterPro; IPR049517; ACX-like_C.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR008040; Hydant_A_N.
DR   InterPro; IPR002821; Hydantoinase_A.
DR   InterPro; IPR045079; Oxoprolinase_fam.
DR   PANTHER; PTHR11365; 5-OXOPROLINASE RELATED; 1.
DR   PANTHER; PTHR11365:SF23; HYPOTHETICAL 5-OXOPROLINASE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF19278; Hydant_A_C; 1.
DR   Pfam; PF05378; Hydant_A_N; 1.
DR   Pfam; PF01968; Hydantoinase_A; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000199170}.
FT   DOMAIN          6..180
FT                   /note="Hydantoinase/oxoprolinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05378"
FT   DOMAIN          200..489
FT                   /note="Hydantoinase A/oxoprolinase"
FT                   /evidence="ECO:0000259|Pfam:PF01968"
FT   DOMAIN          564..658
FT                   /note="Acetophenone carboxylase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19278"
FT   REGION          589..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..612
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   671 AA;  70266 MW;  EDFEFDF1D46AB9BC CRC64;
     MAERIRLGAD VGGTFTDVVL AAGTELVTAK VPSTEEQSVG VVAGIHKACA AAGIDPAAVD
     EFTHAMTVSV NALLERAGAK TALVTTEGFR DVLELGRQDR PDLYDLSATR PEPLVPRRRR
     FEVPERATPD GITTPVDEEA VREVAARIRE SDAESVAVSF LHAYAAPENE RRAVEVLEAE
     LDVPVSASHE VLAEFREYER TATTVVDAYV TPTIDRYLGR LAERAAETGL PEPLVMQANG
     GIAGIETVRD HAVTTTMSGP AAGVVGANAA AGSVARERDL RGLVTFDMGG TSSDVSLVRD
     GEAERTTESE INGQPIRTPM VDVTTVGAGG GSIAWVDDGG ALRVGPRSAG ADPGPACYGK
     GGTEPTVTDA DLVLGYIGES TDLGGELSLD ADAAREALAG LAADADLDGP VAAARGVHRI
     ANATMARAIR AATVERGHDP REFGLVAFGG AGPMHAAALA ADLDIDTVIV PPACGVLSAF
     GLLAADEQHD AVRTHRVAID DVDPATVETH YDALEADVRE DARDPDAASI RRWADLRYAG
     QSFELTVDVA ATFDPARVRE RFHEAHEATY GYRMDEPVAL VNLRVAATAT RSDPRTEHAA
     DGEPRVGERT ARFGDGAGRT TPVYDRSGLA VGSTLDGSAV IEQAESTVVI PPAWEATVRD
     DGSLVLTGVT E
//
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