ID   A0A1H7I9F0_9ACTN        Unreviewed;       863 AA.
AC   A0A1H7I9F0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II {ECO:0000313|EMBL:SEK58472.1};
GN   ORFNames=SAMN04515665_103103 {ECO:0000313|EMBL:SEK58472.1};
OS   Blastococcus sp. DSM 46786.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1798227 {ECO:0000313|EMBL:SEK58472.1, ECO:0000313|Proteomes:UP000198952};
RN   [1] {ECO:0000313|Proteomes:UP000198952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46786 {ECO:0000313|Proteomes:UP000198952};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOAO01000003; SEK58472.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7I9F0; -.
DR   STRING; 1798227.SAMN04515665_103103; -.
DR   Proteomes; UP000198952; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:SEK58472.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198952};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        760..782
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          45..285
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          327..695
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
SQ   SEQUENCE   863 AA;  89589 MW;  7255BE20158571B1 CRC64;
     MTASSPIELP GLDPSWSRWV PVPGADGGKH RWHVLDNGVP DPVGTLLCVH GNPTWSYLWR
     RLVAAAPPGW RVVAPDQLGM GWSDRPAAPR TLAQRVADLG ALTAELGVSG PVVTVAHDWG
     GIISLGWALE HRQDVRGVVL TNTAVAMPEG DLGPALIRLA HAPGLRTAVT QASSVFVRGA
     TALSRPPLPR EVRRAYAQPY DSAERRRAVG EFVADIPFRP GHASRPAQEA IAEGIRSLDV
     PALLLWGPRD PVFGEKYLAD LRERLPRADV HRYEGASHLL PEDAPQYAEA VATWVTDRCG
     ASNAPTPGRG GASAQPARPW AALADRAGDD SPAVVAAGGV PVSWARLARR VSDLAAGLAA
     AGIRPGDRVA LLLEPSTDLT AAVYATWRAG AVIVVADKGL GLRGMRRALR GAAPDHVLGS
     AAGLAAARAM GLPATRILAG PASARLRRAL GAGHDLASLE VLGRTSSAPA EPPLDADCAV
     VFTSGATGPA KGVVYTQRQV GAQLELVRTA YRLTPGDSLV AAFAPFSVLG PGLGIASSVP
     DVDVTAPATL TAAKLADAAA AVDATVVFAA PAALRRVAAT SSDLTEEQRS ALGRVRLLMS
     AGAPVPTPLL RRLGETFPAA EPHTPYGMTE ALPVTDVSLG EIEAAGPGNG ICVGRPVPGV
     EVRISPLSPL GTADGALTGS PDVPGEVCVR AAHVKDRYDA LWATERAAGR DPGWHRTGDV
     GHLDGEGRLW IEGRLAHVLT TADGPMTPVG PELRIEFLDA VAAAAIVGVG PVGAQVAVAV
     VVPPGRARRR LPRADRLTVA PAELAGTVRE VAEIDLAAVL VAGALPVDIR HQSKVDRAVL
     ARRATRVLSG TPVRWASRRS TRP
//