ID A9A3C8_NITMS Unreviewed; 212 AA.
AC A9A3C8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Peptidase C26 {ECO:0000313|EMBL:ABX12557.1};
GN OrderedLocusNames=Nmar_0661 {ECO:0000313|EMBL:ABX12557.1};
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=436308 {ECO:0000313|EMBL:ABX12557.1, ECO:0000313|Proteomes:UP000000792};
RN [1] {ECO:0000313|EMBL:ABX12557.1, ECO:0000313|Proteomes:UP000000792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1 {ECO:0000313|EMBL:ABX12557.1,
RC ECO:0000313|Proteomes:UP000000792};
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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DR EMBL; CP000866; ABX12557.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A3C8; -.
DR STRING; 436308.Nmar_0661; -.
DR EnsemblBacteria; ABX12557; ABX12557; Nmar_0661.
DR KEGG; nmr:Nmar_0661; -.
DR eggNOG; arCOG00088; Archaea.
DR HOGENOM; CLU_030756_5_0_2; -.
DR InParanoid; A9A3C8; -.
DR OrthoDB; 3321at2157; -.
DR PhylomeDB; A9A3C8; -.
DR Proteomes; UP000000792; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR011697; Peptidase_C26.
DR InterPro; IPR044668; PuuD-like.
DR PANTHER; PTHR43235; GLUTAMINE AMIDOTRANSFERASE PB2B2.05-RELATED; 1.
DR PANTHER; PTHR43235:SF1; GLUTAMINE AMIDOTRANSFERASE PB2B2.05-RELATED; 1.
DR Pfam; PF07722; Peptidase_C26; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Reference proteome {ECO:0000313|Proteomes:UP000000792}.
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 189
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 212 AA; 24452 MW; 4E23ECA8650F0851 CRC64;
MVKKIGITLR IETIQEYDEK RDALSHDWFD FFQKLNCLPV LIPNKLREVE SFLEEMDLNG
LILSGGDNIG DDPERDKTEK KIMTFAMTNN IPLLGVCRGM QVINQFFNGK IIFDNSNIHV
GKNHVVDIID TKFSNFLQTN TMNVNSFHHN LIDKSSLGKN LIPFAFSSID QTIEGFYHEN
SPILGVMWHP ERVNLNSNQT ELVNMLYCDK IW
//
