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Database: UniProt
Entry: Q989S8_RHILO
LinkDB: Q989S8_RHILO
Original site: Q989S8_RHILO 
ID   Q989S8_RHILO            Unreviewed;       407 AA.
AC   Q989S8;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   SubName: Full=Putative carboxylase {ECO:0000313|EMBL:BAB52616.1};
GN   OrderedLocusNames=mlr6296 {ECO:0000313|EMBL:BAB52616.1};
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB52616.1, ECO:0000313|Proteomes:UP000000552};
RN   [1] {ECO:0000313|EMBL:BAB52616.1, ECO:0000313|Proteomes:UP000000552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC   {ECO:0000313|Proteomes:UP000000552};
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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DR   EMBL; BA000012; BAB52616.1; -; Genomic_DNA.
DR   RefSeq; WP_010913935.1; NC_002678.2.
DR   AlphaFoldDB; Q989S8; -.
DR   KEGG; mlo:mlr6296; -.
DR   PATRIC; fig|266835.9.peg.5003; -.
DR   eggNOG; COG0026; Bacteria.
DR   HOGENOM; CLU_029016_6_2_5; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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; PF13535; ATP-grasp_4; 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          114..306
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   407 AA;  44473 MW;  6F874D646D531FF0 CRC64;
     MAKRALILVE GSRTGLLYVQ AAQRLGLSPI TLSADPTQYD YIAAEGIEAI HVDTADLDAL
     IGECSRLRAT YEIAGITCAK ESVYATVAKL CRHFDLPGPN PTSIERCCDK FTQRQLLAEA
     GVPVPSYRLA ANAADIESYA AEIGLPVILK PAVGVGSSGV RLCRNGDELA EHTTYLLGGK
     HIWRSSPRIL VEEFAQGPYY STEIMGDEVI GIYAGEFGPE PYFVFREFTL PALLTDEEQE
     RIVDVSLGCL RALGLGWGPT CIEFRWTKRG PVVIEVNPRL GGAPGPQLVQ LTYGLDLVTE
     HIKLVIGEKW DLRRRHSHTA AARILVPDRD GTLDWIDGDN RATAVPGVAE VEFYIGPNTP
     IVRKGDHRDW IGHVIVASPS RALTEATLHR AVDLIDWSIA PFPTLGE
//
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