ID A0A0W0ZX08_9GAMM Unreviewed; 379 AA.
AC A0A0W0ZX08;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000313|EMBL:KTD73328.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:KTD73328.1};
GN Name=carB_1 {ECO:0000313|EMBL:KTD73328.1};
GN ORFNames=Ltuc_1175 {ECO:0000313|EMBL:KTD73328.1};
OS Legionella tucsonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=40335 {ECO:0000313|EMBL:KTD73328.1, ECO:0000313|Proteomes:UP000054693};
RN [1] {ECO:0000313|EMBL:KTD73328.1, ECO:0000313|Proteomes:UP000054693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49180 {ECO:0000313|EMBL:KTD73328.1,
RC ECO:0000313|Proteomes:UP000054693};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KTD73328.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LNZA01000001; KTD73328.1; -; Genomic_DNA.
DR RefSeq; WP_058520376.1; NZ_LNZA01000001.1.
DR AlphaFoldDB; A0A0W0ZX08; -.
DR STRING; 40335.Ltuc_1175; -.
DR PATRIC; fig|40335.7.peg.1240; -.
DR OrthoDB; 40611at2; -.
DR Proteomes; UP000054693; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003806; ATP-grasp_PylC-type.
DR Pfam; PF02655; ATP-grasp_3; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:KTD73328.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000054693}.
FT DOMAIN 117..287
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 379 AA; 44178 MW; BD54F28D6444773C CRC64;
MNILVTGGRA PATMDIMRSL INQGYEVYSA ESMLYPLARF VKGVSKHFVI PKPNQDLTAF
LKAIKEIVIQ YKIDLLIPTC EEIFYISQGY EELSKHTKLL CEPFERLSQL HNKYTFNQLV
NEYNLTAPQS WLMNTDKDKQ ILPNEALVLK PVFSRFGSRT LIKPSKKIIS ELAINEPYIA
QHYIQGKEYS AYAIVHKGEV LIQSCYYSKY QAGRSTGIYF EPVEIKPITE FIKTFCKCFQ
FSGQIAFDFI LVNDKAYVLE CNPRVTSGFH LLTDKIDWYT ILSGQRQYDI PNMKYMQPYM
LGQGMMLHCL KYIPKKPRQF IKDYQRAHDV LRHKAYPWLR LKSILMMLNV LCRAIRVKKG
FYPASTYDID FNGVENLFK
//
