ID Q98JC6_RHILO Unreviewed; 559 AA.
AC Q98JC6;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:BAB49240.1};
GN OrderedLocusNames=mlr2005 {ECO:0000313|EMBL:BAB49240.1};
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:BAB49240.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB49240.1, 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).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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; BA000012; BAB49240.1; -; Genomic_DNA.
DR AlphaFoldDB; Q98JC6; -.
DR KEGG; mlo:mlr2005; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_59_10_5; -.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR CDD; cd05973; MACS_like_2; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43605:SF10; ACYL-COA SYNTHETASE MEDIUM CHAIN FAMILY MEMBER 3; 1.
DR PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598}.
FT DOMAIN 62..404
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 466..543
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 559 AA; 60017 MW; DBD739E3162C5BD2 CRC64;
MGRWAPPGRT DMTGLPRYED AVARFRIEDE IARLDGDPLT GINGYVECCG RHTGQNRLAL
RAISAGGELR LFSFDDLADM SGRVGNLLKD AGVGPGDVVA GMLPRIPELI ALILGTWRIG
AIYQPLFTAF GPKAIEHRLG YSGAKLVVTN PANRGKLDEM KTCPPIATIL GPGDPLPAGD
IDFRAALAAA SPDCEPVMRK GEDLFMMMST SGTTGLPKGV PVPLNALLSF GAYIRDAIGL
RPDDVFWNIA DPGWAYGLYY AITGPLLLGI ATTFNEGAFN AGNTYDVIER LGVTSLAGSP
TAFRLLLAEG PEAAARIKGR LRVVSSAGEP LNPEVIRWFD AHLAAPIHDH YGQTENGMMV
NNHHGLAHAV RAGSAGFAMP GYRMVVLDDE GNELGLNQPG ILAVDVANSP LRWFDGYHQA
ETPAIAGGYY RTGDTVEYEP DGSVSFIGRA DDVITSSGYR IGPFDVESAL IEHPAVNEAA
VVGVPDPQRT EIVKAFVILA PAYQGSTELA EELAQHVRKR LSAHAYPREI DFVAELPKTP
SGKIQRFLLR QAEVEKRKG
//
