ID S3WV70_9ACTN Unreviewed; 563 AA.
AC S3WV70;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=(2,3-dihydroxybenzoyl)adenylate synthase {ECO:0000313|EMBL:EPH02564.1};
GN ORFNames=HMPREF1531_01872 {ECO:0000313|EMBL:EPH02564.1};
OS Propionibacterium sp. oral taxon 192 str. F0372.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=1203605 {ECO:0000313|EMBL:EPH02564.1, ECO:0000313|Proteomes:UP000014567};
RN [1] {ECO:0000313|EMBL:EPH02564.1, ECO:0000313|Proteomes:UP000014567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0372 {ECO:0000313|EMBL:EPH02564.1,
RC ECO:0000313|Proteomes:UP000014567};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Socransky S.S.,
RA Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Propionibacterium sp. oral taxon 192 str. F0372.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPH02564.1}.
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DR EMBL; ATFL01000014; EPH02564.1; -; Genomic_DNA.
DR RefSeq; WP_016669660.1; NZ_KE340297.1.
DR AlphaFoldDB; S3WV70; -.
DR STRING; 1203605.HMPREF1531_01872; -.
DR PATRIC; fig|1203605.3.peg.1932; -.
DR eggNOG; COG1021; Bacteria.
DR HOGENOM; CLU_000022_59_7_11; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000014567; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016877; F:ligase activity, forming carbon-sulfur bonds; 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; 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000014567}.
FT DOMAIN 40..404
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 456..533
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 563 AA; 59480 MW; 15A419E36D059EAA CRC64;
MSIIRPATTG RSDISRIAAE VSAHVASGIF LDATLLDLLD VQVRERGNVE AVLDARESLT
FAELRREIDT TAAHLIGAGI MSGQLVLVQM PNSADYLKVL FGCMVIGAVP VLMLISHRHR
ELLHVARITG ATAIITVDEH LGVDHAAMAC RVAEELAVQV LVVGDRVPAG ARALYATTPG
DLGAVAGPTV GDTALCLLSG GTTSKPKVIP RLHGAYACVA LASARRCQVT PDDTYLAVLS
TSHDYPLSSP GVLGVLLNGG RVIMSVTASF DEVANWLETE EVTLVQAVPA VAAAWAQAAE
QAPADLRAEW HIPTLVLGAA KVGTELASRL VKIFGCRIIQ GYGLGEGITC FTSPDDPDEI
AWNTQGTPVS DQDEVRILDP QGNVLGPGEV GELVEKGPYT FHGYMGAPEL NAACFDNEGF
FHTGDQAMIR HDGRVVITGR VHEQINRAGE NVIPSEVESL VAAHPDVNEV AVFGIPDSEM
GEATCAVVTV FPGREQPTRA TMAAFLHASG VGAYKVPDRL VVVRAMPRKN IGKIDKLILR
SQILGGAEAA GPSTGIEKKD NHE
//
