ID K4KIV1_SIMAS Unreviewed; 256 AA.
AC K4KIV1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Putative glutamine amidotransferase {ECO:0000313|EMBL:AFU98120.1};
GN OrderedLocusNames=M5M_04565 {ECO:0000313|EMBL:AFU98120.1};
OS Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Simiduia.
OX NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFU98120.1, ECO:0000313|Proteomes:UP000000466};
RN [1] {ECO:0000313|EMBL:AFU98120.1, ECO:0000313|Proteomes:UP000000466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC {ECO:0000313|Proteomes:UP000000466};
RX PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT bacterium able to degrade a variety of polysaccharides.";
RL Genome Announc. 1:E00039-E00039(2013).
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DR EMBL; CP003746; AFU98120.1; -; Genomic_DNA.
DR RefSeq; WP_015046293.1; NZ_ATUQ01000013.1.
DR AlphaFoldDB; K4KIV1; -.
DR STRING; 1117647.M5M_04565; -.
DR KEGG; saga:M5M_04565; -.
DR eggNOG; COG2071; Bacteria.
DR HOGENOM; CLU_030756_0_0_6; -.
DR OrthoDB; 9813383at2; -.
DR Proteomes; UP000000466; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01745; GATase1_2; 1.
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 ECO:0000313|EMBL:AFU98120.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000466};
KW Transferase {ECO:0000313|EMBL:AFU98120.1}.
FT ACT_SITE 116
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 226
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 256 AA; 27519 MW; FF3308558E5E913C CRC64;
MRRPVIAITA ETLDKTKGAD TTRYYQVMAK YVAPVAEIMG ALPLIVPPLA DKLDRETLLA
SVDGILLTGG VSNIEPHHYQ GGASYAGCPH DPARDATVLP MIKDIVQRGI PLFGICRGFQ
EMNVAYGGDL FQQLHVEADF ALHNTTVDFD APADGLYADV HDLNLAQGGL LARIANGPVQ
KVNSIHGQGI KTLGAGLQVE GTAPDGLIEA FSVTDAKQFA LAVQWHPEWK PANNPLYMAM
WQAFKTAAET YAANRG
//
