(data stored in SCRATCH zone)

SWISSPROT: E6V1D7_VARPE

ID   E6V1D7_VARPE            Unreviewed;       330 AA.
AC   E6V1D7;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 50.
DE   RecName: Full=Formamidase {ECO:0000256|HAMAP-Rule:MF_01243};
DE            EC=3.5.1.49 {ECO:0000256|HAMAP-Rule:MF_01243};
DE   AltName: Full=Formamide amidohydrolase {ECO:0000256|HAMAP-Rule:MF_01243};
GN   Name=amiF {ECO:0000256|HAMAP-Rule:MF_01243};
GN   OrderedLocusNames=Varpa_0279 {ECO:0000313|EMBL:ADU34501.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34501.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34501.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34501.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
CC   -!- FUNCTION: Is an aliphatic amidase with a restricted substrate
CC       specificity, as it only hydrolyzes formamide. {ECO:0000256|HAMAP-
CC       Rule:MF_01243}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=formamide + H2O = formate + NH4(+); Xref=Rhea:RHEA:21948,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15740, ChEBI:CHEBI:16397,
CC         ChEBI:CHEBI:28938; EC=3.5.1.49; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01243};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       Aliphatic amidase family. {ECO:0000256|HAMAP-Rule:MF_01243}.
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DR   EMBL; CP002417; ADU34501.1; -; Genomic_DNA.
DR   RefSeq; WP_013538747.1; NC_014931.1.
DR   STRING; 595537.Varpa_0279; -.
DR   EnsemblBacteria; ADU34501; ADU34501; Varpa_0279.
DR   GeneID; 29715883; -.
DR   KEGG; vpe:Varpa_0279; -.
DR   eggNOG; ENOG4105DCY; Bacteria.
DR   eggNOG; COG0388; LUCA.
DR   HOGENOM; HOG000077502; -.
DR   KO; K01455; -.
DR   OMA; RIWGCFS; -.
DR   OrthoDB; 1650683at2; -.
DR   BioCyc; VPAR595537:G1GQO-281-MONOMER; -.
DR   Proteomes; UP000008917; Chromosome.
DR   GO; GO:0004328; F:formamidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.60.110.10; -; 1.
DR   HAMAP; MF_01243; Formamidase; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR022843; Formamidase.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; E6V1D7.
DR   SWISS-2DPAGE; E6V1D7.
KW   Acyltransferase {ECO:0000313|EMBL:ADU34501.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01243};
KW   Lipoprotein {ECO:0000313|EMBL:ADU34501.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   Transferase {ECO:0000313|EMBL:ADU34501.1}.
FT   DOMAIN       14    256       CN hydrolase. {ECO:0000259|PROSITE:
FT                                PS50263}.
FT   ACT_SITE     60     60       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01243}.
FT   ACT_SITE    129    129       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01243}.
FT   ACT_SITE    162    162       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01243}.
SQ   SEQUENCE   330 AA;  35906 MW;  02DA2F99C1C1B272 CRC64;
     MSGLGGLNKS AHGVVVGLVQ LQLPNVKTPA DLAAQTQRIC DMVGKARRNQ STMDLVVFPE
     YALHGLSMDT NPEIMCTLDG PEVAAFKRAC IEHRIWGCFS IMEANPGGNP YNSGLVIDDQ
     GEIKLYYRKL HPWVPVEPWE PGNLGIPVCD GPNGSKLALI ICHDGMFPEM AREAAYKGAD
     IILRTAGYTA PIRHAWKITN QANAFCNLAY TASVCLCGSD GSFDSMGEGM FCNFDGTVLV
     EGGGRVDEII TAELRPDLVR EARTGWGVEN NIYQLYHRGY VAVKGGAQDC PYTYMHDMAA
     GTYRLPWSAD VKVTDGTSCG FAPPERNYQG
//

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