ID Q8NTA7_CORGL Unreviewed; 568 AA.
AC Q8NTA7; Q6M7W2;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE SubName: Full=Acyl-CoA synthetases (AMP-forming)/AMP-acid ligases II {ECO:0000313|EMBL:BAB97793.1};
DE EC=6.2.1.3 {ECO:0000313|EMBL:BAB97793.1};
GN OrderedLocusNames=Cgl0400 {ECO:0000313|EMBL:BAB97793.1};
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627 {ECO:0000313|EMBL:BAB97793.1, ECO:0000313|Proteomes:UP000000582};
RN [1] {ECO:0000313|Proteomes:UP000000582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC NCIMB 10025 {ECO:0000313|Proteomes:UP000000582};
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
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; BA000036; BAB97793.1; -; Genomic_DNA.
DR RefSeq; NP_599647.1; NC_003450.3.
DR RefSeq; WP_003855494.1; NC_006958.1.
DR AlphaFoldDB; Q8NTA7; -.
DR STRING; 196627.cg0480; -.
DR GeneID; 69620865; -.
DR KEGG; cgl:Cgl0400; -.
DR PATRIC; fig|196627.13.peg.400; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_7_11; -.
DR OrthoDB; 9803968at2; -.
DR BioCyc; CORYNE:G18NG-9957-MONOMER; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR CDD; cd05936; FC-FACS_FadD_like; 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; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43767:SF1; NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:BAB97793.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000582}.
FT DOMAIN 38..427
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 477..552
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 568 AA; 62688 MW; 877856CFEEAC5384 CRC64;
MSAYETKEWL QHYPEWTPHS LEYGDTTLLD VYDNNLAINA DKPATYFFGR SQTYGELDKE
VRKTAAGLRA LGVRPGDHVA IILPNCPQHI AAFYAVLKLG AVVIEHNPLY TAHELLEPFK
DHGARVAIVW DKASPTVEQL RGQTQLETIV SVNMINAMPP LQRLALRLPI PALRKSRESL
SGAAPNTVPF ETLTSAAMGG DGDDVVSEPT VTKESVALIL YTSGTTGRPK GAQLTHGNLF
SNLLQGKHWV PGLGDKPERM LAALPMFHAY GLTMVGTLSV FIGGEMVLLP TPRIDLIMNV
MKKHTPTWLP GVPTLYEKIV DASEKEGIPI KGVRNAFSGA STLSQRTVER WEKHTGGRLV
EGYGLTETSP IIVGNPMSDH RRQGYVGIPF PDTIVRIANP ENLDETMPDG SEGEVLVKGP
QVFKGYLNQE EATKNSFHGE WYRTGDVGVM EEDGFIRLVA RIKEVIITGG FNVYPAEVEE
VLAEHPDIED SAVVGIPRED GSENVVAAIT LVEGAALDPD GLKEFARKNL TRYKVPRTFY
HFEEMPRDQM GKIRRREVQA ELLKKLGK
//