ID V6IV12_9BACL Unreviewed; 247 AA.
AC V6IV12;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Glutamine amidotransferase {ECO:0000313|EMBL:EST10957.1};
GN ORFNames=P343_14155 {ECO:0000313|EMBL:EST10957.1};
OS Sporolactobacillus laevolacticus DSM 442.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=1395513 {ECO:0000313|EMBL:EST10957.1, ECO:0000313|Proteomes:UP000018296};
RN [1] {ECO:0000313|EMBL:EST10957.1, ECO:0000313|Proteomes:UP000018296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 442 {ECO:0000313|EMBL:EST10957.1,
RC ECO:0000313|Proteomes:UP000018296};
RX PubMed=24371202;
RA Wang H., Wang L., Ju J., Yu B., Ma Y.;
RT "Genome Sequence of Sporolactobacillus laevolacticus DSM442, an Efficient
RT Polymer-Grade D-Lactate Producer from Agricultural Waste Cottonseed as a
RT Nitrogen Source.";
RL Genome Announc. 1:e01100-13(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EST10957.1}.
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DR EMBL; AWTC01000015; EST10957.1; -; Genomic_DNA.
DR RefSeq; WP_023511062.1; NZ_AWTC01000015.1.
DR AlphaFoldDB; V6IV12; -.
DR STRING; 1395513.P343_14155; -.
DR PATRIC; fig|1395513.3.peg.2869; -.
DR eggNOG; COG2071; Bacteria.
DR OrthoDB; 9813383at2; -.
DR Proteomes; UP000018296; Unassembled WGS sequence.
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:EST10957.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018296};
KW Transferase {ECO:0000313|EMBL:EST10957.1}.
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 216
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 247 AA; 27074 MW; 32DAAC46F88EFCD1 CRC64;
MTKPIIGITS GFVKLSNFSE GDYAHQDYIT SLIKAGAVPL ILPIAPGPCV DQYAELCDGF
LLSGGCDVNP QYFGEDPSPG CGVFDTERDE AEFQLVRLAI KKSKPVFGIC RGLQVMNVAL
GGTLIQDIPS ELDHPIQHEQ KVPRRQGSHR VSLEKETQLY KVLKEQESIV VNSLHHQSID
RLGDGLRTAA FSSDGIIEAI DMTDNGLLMG VQWHPESMTA GGSELMLDLF KHFVDTCKEM
KQANSEV
//
