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Database: UniProt
Entry: C6WIH2_ACTMD
LinkDB: C6WIH2_ACTMD
Original site: C6WIH2_ACTMD 
ID   C6WIH2_ACTMD            Unreviewed;       555 AA.
AC   C6WIH2;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:ACU36215.1};
GN   OrderedLocusNames=Amir_2275 {ECO:0000313|EMBL:ACU36215.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS   / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU36215.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU36215.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC   NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA   Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA   Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; CP001630; ACU36215.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6WIH2; -.
DR   STRING; 446462.Amir_2275; -.
DR   KEGG; ami:Amir_2275; -.
DR   eggNOG; COG0365; Bacteria.
DR   HOGENOM; CLU_000022_59_10_11; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000002213; 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; 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, ECO:0000313|EMBL:ACU36215.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213}.
FT   DOMAIN          42..398
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          449..526
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
FT   REGION          528..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   555 AA;  61190 MW;  4503A895493040F0 CRC64;
     MDFRQARDFL LQHADDHDAA RAGFAWPDLA EFNWALDWFD EIARDNDRTA LWIVEEDGSE
     GRWSFAELSR RSAQVANWLR GNGVARGDRV VLMLGNQVQL WETLLGAMKL GAVVIPATTL
     LGPEDLRDRI ERGGARHVVV TSGDAPKFAE VPGDYTRIAV GAPVDGWLDF ADSERADAAF
     TPDAPTRADD TLLLYFTSGT TAAPKLVEHT HVSYPVGHLS TMYWQGLRPG DVHLNISSPG
     WAKHAWSNVF APWNAEATVF VHNYRRFDAA RLMAEMDRCG VTSFCAPPTV WRMLIQADLT
     ALRVPPRKAV GAGEPLNPEV IEQVAKAWGV TVRDGFGQTE TTVQIANTPG QPVKPGSMGR
     PAPGYEVVLV DPITGEPGTE GEICLDLSRR PLGLMVGYHG DPERTAEVMR GGYYHTGDVA
     SVDEDGHLTY VGRTDDLFKS SDYRISPFEL ESVLLEHDAV AEAAVVPSPD PVRLAVPKAH
     VVLAPGWEPT AETALAVLRH ARERLAPYKR VRRLEFGPLP KTISGKIRRV ELREQEDGGR
     PDGEHREEDF PQLRG
//
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