ID H9ZZQ7_FERFK Unreviewed; 656 AA.
AC H9ZZQ7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=5-oxoprolinase (ATP-hydrolyzing) {ECO:0000313|EMBL:AFH42214.1};
GN OrderedLocusNames=FFONT_0223 {ECO:0000313|EMBL:AFH42214.1};
OS Fervidicoccus fontis (strain DSM 19380 / JCM 18336 / VKM B-2539 / Kam940).
OC Archaea; Thermoproteota; Thermoprotei; Fervidicoccales; Fervidicoccaceae;
OC Fervidicoccus.
OX NCBI_TaxID=1163730 {ECO:0000313|EMBL:AFH42214.1, ECO:0000313|Proteomes:UP000007391};
RN [1] {ECO:0000313|Proteomes:UP000007391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC {ECO:0000313|Proteomes:UP000007391};
RA Lebedinsky A.V., Mardanov A.V., Gumerov V.M., Beletsky A.V., Kublanov I.V.,
RA Perevalova A.A., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Fervidicoccus fontis complete genome analysis confirms its distinct
RT phylogenetic position and predicts its environmental function.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFH42214.1, ECO:0000313|Proteomes:UP000007391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19380 / VKM B-2539 / Kam940
RC {ECO:0000313|Proteomes:UP000007391};
RX PubMed=24366681; DOI=10.1007/s00792-013-0616-7;
RA Lebedinsky A.V., Mardanov A.V., Kublanov I.V., Gumerov V.M., Beletsky A.V.,
RA Perevalova A.A., Bidzhieva S.Kh., Bonch-Osmolovskaya E.A., Skryabin K.G.,
RA Ravin N.V.;
RT "Analysis of the complete genome of Fervidococcus fontis confirms the
RT distinct phylogenetic position of the order Fervidicoccales and suggests
RT its environmental function.";
RL Extremophiles 18:295-309(2014).
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DR EMBL; CP003423; AFH42214.1; -; Genomic_DNA.
DR AlphaFoldDB; H9ZZQ7; -.
DR STRING; 1163730.FFONT_0223; -.
DR KEGG; ffo:FFONT_0223; -.
DR eggNOG; arCOG01511; Archaea.
DR HOGENOM; CLU_002157_1_2_2; -.
DR InParanoid; H9ZZQ7; -.
DR OrthoDB; 8261at2157; -.
DR Proteomes; UP000007391; Chromosome.
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:UP000007391}.
FT DOMAIN 5..176
FT /note="Hydantoinase/oxoprolinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05378"
FT DOMAIN 195..486
FT /note="Hydantoinase A/oxoprolinase"
FT /evidence="ECO:0000259|Pfam:PF01968"
FT DOMAIN 518..647
FT /note="Acetophenone carboxylase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19278"
SQ SEQUENCE 656 AA; 72293 MW; 843F47B5A5787477 CRC64;
MPKVVGIDTG GTFTDFVYIK DDGSIGFFKS LSTPKSPEDA VIEGLKALGS GETVIHATTL
GTNAIRGQFG IEIPKLSLVT TRGFKGVIEI GRQNRPKLYD IFFEKPKPLV ERDFIFEANE
RIDAFGRVLE KIREEQIEEI GSKLKEAGVS SVAISFLHSY INPSHEKTAE RILSKYVEYV
SPSYLVSPEP REYERTSSAL VNAALMPIIS KYIERLNKRL KELNVKELLV MSSSGGIVDA
EEASKRPVQL VESGPAAGVV ATAELCRMMG INKAISFDMG GTTAKAGTIV NYEFEITSEY
EVGGESNHGR MIKGSGYSVR FPFIDLAEVS AGGGTIIWRD DAGALRIGPK SAGADPGPAC
YDRGGKYPTL TDANLVLGRI GESLLGGKMK IRKDLAIKAL SSLGEPVEIA NRSIKLADLE
MARAIRLVTV ERGIDPEEFV LFAFGGAGPQ FAAELANEIG IKKIVIPPHP GVFSALGLLM
ADWRFEDRTA FPKDIEMAYR NMEEKLLKKV GRVDYFIRYA DVRYVGQGWE LTVPVGSPVD
IKEIKKTFNK KHFSTYGFML ESDIEVVLAR VFAVSKREKP LFSAPKIRAS GRAKGYRKVY
MNGEWIETPI YCRYSLDEGF KAEGPLLIDE YDTTTFVPSG WRVSVGAFSE LILERM
//
