ID E8THQ6_MESCW Unreviewed; 428 AA.
AC E8THQ6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding protein {ECO:0000313|EMBL:ADV14818.1};
GN OrderedLocusNames=Mesci_5771 {ECO:0000313|EMBL:ADV14818.1};
OS Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 /
OS WSM1271).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV14818.1, ECO:0000313|Proteomes:UP000007471};
RN [1] {ECO:0000313|Proteomes:UP000007471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 2942 / LMG 23838 / WSM1271
RC {ECO:0000313|Proteomes:UP000007471};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Nandasena K., Reeve W.G., Howieson J.G., O'Hara G.,
RA Tiwari R.P., Woyke T.;
RT "Complete sequence of chromosome of Mesorhizobium ciceri bv. biserrulae
RT WSM1271.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002447; ADV14818.1; -; Genomic_DNA.
DR RefSeq; WP_013533467.1; NC_014923.1.
DR RefSeq; YP_004144868.1; NC_014923.1.
DR AlphaFoldDB; E8THQ6; -.
DR STRING; 765698.Mesci_5771; -.
DR KEGG; mci:Mesci_5771; -.
DR PATRIC; fig|765698.3.peg.6278; -.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_029016_6_2_5; -.
DR OrthoDB; 9765608at2; -.
DR Proteomes; UP000007471; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR040570; LAL_C2.
DR PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF18603; LAL_C2; 1.
DR SMART; SM01209; GARS_A; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 118..308
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 405..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 46498 MW; F61A2F71980B6389 CRC64;
MTRRALILVE GHNRIGLLYM KAAQRLGLHP ITLSADPARY DYLAAESIET IRVDTNSLDA
LIYECSRLGG TYDIAGITGF AGDDESIYAT VGQLCRYFDL PGPNPASIEG CCNKFTQRQL
LAEAGVPMPS YRLAANAAEV ESAVAQIGLP VVIKPALGSG SIGVRLCRNV DDLAEHATYL
LSGRHRSSPR ILVEEFAQGP HYSADIMGNE VIGIEAAEFG PPPHFIFREY IHPAPLTSEE
YKCIADLSLS CLRALGLGWG PSFVEFRWTK RGPVVIEVNP RIAGGANPQL VQLAYGVDLV
TEHIKLTVGE GSDLRKKYSH SAGARFLIAD RDGTLDWISG DCQAAGLPGV AEVELYAKPK
TPIVRKGDYR DRIGHVVAAS PSYSETETIL EGAVNLINWS ITPFPTSGEQ EQSEAPHPPH
QRRKLRNG
//
