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Database: UniProt/TrEMBL
Entry: A0A0D5AEI5_9NOCA
LinkDB: A0A0D5AEI5_9NOCA
Original site: A0A0D5AEI5_9NOCA 
ID   A0A0D5AEI5_9NOCA        Unreviewed;       562 AA.
AC   A0A0D5AEI5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acetyl-coenzyme A synthetase {ECO:0000313|EMBL:AJW41256.1};
GN   ORFNames=NY08_3246 {ECO:0000313|EMBL:AJW41256.1};
OS   Rhodococcus sp. B7740.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1564114 {ECO:0000313|EMBL:AJW41256.1, ECO:0000313|Proteomes:UP000032410};
RN   [1] {ECO:0000313|EMBL:AJW41256.1, ECO:0000313|Proteomes:UP000032410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7740 {ECO:0000313|EMBL:AJW41256.1};
RX   PubMed=25931596;
RA   Zhang D., Li L., Zhu S., Zhang N., Yang J., Ma X., Chen J.;
RT   "Complete Genome Sequence of Rhodococcus sp. B7740, a Carotenoid-Producing
RT   Bacterium Isolated from the Arctic Sea.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; CP010797; AJW41256.1; -; Genomic_DNA.
DR   RefSeq; WP_045200539.1; NZ_CP010797.1.
DR   AlphaFoldDB; A0A0D5AEI5; -.
DR   STRING; 1564114.NY08_3246; -.
DR   KEGG; rhb:NY08_3246; -.
DR   PATRIC; fig|1564114.4.peg.3204; -.
DR   HOGENOM; CLU_000022_59_10_11; -.
DR   Proteomes; UP000032410; Chromosome.
DR   GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR   GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
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; 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.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598}.
FT   DOMAIN          52..404
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          454..531
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   562 AA;  61950 MW;  FDA385520D5A4FCF CRC64;
     MAESAYTAFR NARDLLLDAY GEYDRAVDTF EWPSFGETFN WAIDWFDAIA RGNDGTALWI
     VEEDGSEAKY SFDDIARRSD QVARWLEQQG IGRGDSVILM LGNQVELWEA MLAVMKLGAV
     LMPTTTAIGS SDLTDRVVRG NARAVIVNPS DTGKFDDVPG DYLRIATSAS DGWVDYSGAR
     DVEARSFESM TAPTDRLLMY FTSGTTSKPK LVEHTQISYP VGHLSTMYFL GLRPGDVHLN
     ISSPGWAKHA WSCFFAPWIA EATIFIYNYG KFDAKALLEQ IRRAEVTTFC APPTVWRMLI
     QADLAGGGGA LREAIGAGEP LNPEVISRVQ QEWGLSIRDG FGQTETTALV ANTPGAVLKS
     GSMGRPLPGV PVVIVDPTTG ELADEGEICL DLAQHPFNLM TGYLGDPERN AAVMADGYYH
     TGDVASRDSE GYITYVGRTD DVFKASDYKI SPFELESVLI EHPAVAEAAV VPAPDETRLA
     VPKAYVALAS GWEPNEDTAF EILKYAREHL APFLRVRRIE FFELPKTISG KIRRVELRAR
     EDAAVGPLET EWRDDQFPAL KR
//
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