ID D9Q1Z4_ACIS3 Unreviewed; 506 AA.
AC D9Q1Z4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Acyl-CoA ligase (Acyl-CoA synthetase) {ECO:0000313|EMBL:ADL19332.1};
GN OrderedLocusNames=ASAC_0926 {ECO:0000313|EMBL:ADL19332.1};
OS Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 /
OS 345-15).
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC Acidilobus.
OX NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL19332.1, ECO:0000313|Proteomes:UP000000346};
RN [1] {ECO:0000313|EMBL:ADL19332.1, ECO:0000313|Proteomes:UP000000346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15
RC {ECO:0000313|Proteomes:UP000000346};
RX PubMed=20581186; DOI=10.1128/AEM.00599-10;
RA Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "The genome sequence of the crenarchaeon Acidilobus saccharovorans supports
RT a new order, Acidilobales, and suggests an important ecological role in
RT terrestrial acidic hot springs.";
RL Appl. Environ. Microbiol. 76:5652-5657(2010).
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DR EMBL; CP001742; ADL19332.1; -; Genomic_DNA.
DR RefSeq; WP_013266844.1; NC_014374.1.
DR AlphaFoldDB; D9Q1Z4; -.
DR STRING; 666510.ASAC_0926; -.
DR GeneID; 9499166; -.
DR KEGG; asc:ASAC_0926; -.
DR eggNOG; arCOG00857; Archaea.
DR HOGENOM; CLU_000022_59_0_2; -.
DR InParanoid; D9Q1Z4; -.
DR Proteomes; UP000000346; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; PTHR24096:SF149; 4-COUMARATE--COA LIGASE 1-RELATED; 1.
DR PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 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 Ligase {ECO:0000313|EMBL:ADL19332.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000346}.
FT DOMAIN 44..388
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 439..506
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 506 AA; 55881 MW; 1974D72B7FA35548 CRC64;
MEKIWIRLFE GGLPELEPVE EPIHSLLDNV WRGHEGECAA LQLETGSCYT WGALRRASAK
VAGFLRSLGV NEGDQVLFAA NNRIEALAGL LGIWRSSAIS VLVDPLTISE DLYEQLRGRG
IKVGVVSQQF YEREQKTMAR AGVEEVLVVD GQPKEGEVKV HTMSDVIRSD EIYGDDVKSS
SRSLVMYYAG IAGRTMQVYH THRALSTAVK ALADSMKLDF RPVSIVVAPM THVLGLQVST
LTPLYLRGSV VLMQRWSDVA ALEAIRIYGI NFISGAPTMH DSLVEAAKSR GAPPGVRLGL
SGGAPLRPET QEGFRSAFGA PLVQFYGMTE SWVLTYQPTT VGEVKGTVGA PIAGVDIMIV
NPDNPTEEKG PGETGELLAK APWLMEAYED PEETSKAFYN GWLRTGDLMS IDERGLLYFR
GVRKRMIKYK AYPIFPRDLE AVLMRHPDVQ QAYVYGERDP AVGEKPVAKV VLRPGASVTE
KDLLDFVNSQ VAFYKKLHKI YFVDKL
//
