ID Q5FHX3_LACAC Unreviewed; 242 AA.
AC Q5FHX3;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Glutamine amidotransferase {ECO:0000313|EMBL:AAV43701.1};
GN OrderedLocusNames=LBA1903 {ECO:0000313|EMBL:AAV43701.1};
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621 {ECO:0000313|Proteomes:UP000006381};
RN [1] {ECO:0000313|EMBL:AAV43701.1, ECO:0000313|Proteomes:UP000006381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM
RC {ECO:0000313|Proteomes:UP000006381};
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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DR EMBL; CP000033; AAV43701.1; -; Genomic_DNA.
DR RefSeq; WP_011254611.1; NC_006814.3.
DR RefSeq; YP_194732.1; NC_006814.3.
DR AlphaFoldDB; Q5FHX3; -.
DR STRING; 272621.LBA1903; -.
DR GeneID; 56943452; -.
DR KEGG; lac:LBA1903; -.
DR PATRIC; fig|272621.13.peg.1808; -.
DR eggNOG; COG2071; Bacteria.
DR HOGENOM; CLU_030756_2_1_9; -.
DR OrthoDB; 9813383at2; -.
DR BioCyc; LACI272621:G1G49-1857-MONOMER; -.
DR Proteomes; UP000006381; 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:AAV43701.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006381};
KW Transferase {ECO:0000313|EMBL:AAV43701.1}.
FT ACT_SITE 115
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 219
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 242 AA; 26831 MW; 3DD3DB55D970D91E CRC64;
MNKPIIGISG SVIIDDGGIF PGYHRSYVNE DYVDSVVQNG GVPYIIPFTE DDKVIREQLN
NVQGLILSGG HDVDPRFYGE EPLQKIGATW PERDHFDMRL LKLAEENGIP VLGICRGAQI
INVAHGGTLY QDLSYRDGLT LKHMQGHTPS LPTHGMKVNA DSKLAEILGE TEFRVNSFHH
QLIKDVAPDL MVSATAPDGV VEGLENKKGN VIAVQWHPEM LHRNPDVAFM NNLFKFVIDN
AK
//
