ID Q5V5M8_HALMA Unreviewed; 533 AA.
AC Q5V5M8;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000313|EMBL:QCP92959.1};
DE SubName: Full=Medium-chain acyl-CoA ligase {ECO:0000313|EMBL:AAV45174.1};
GN Name=alkK1 {ECO:0000313|EMBL:AAV45174.1};
GN OrderedLocusNames=rrnAC0098 {ECO:0000313|EMBL:AAV45174.1};
GN ORFNames=E6P14_19595 {ECO:0000313|EMBL:QCP92959.1};
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569 {ECO:0000313|EMBL:AAV45174.1, ECO:0000313|Proteomes:UP000001169};
RN [1] {ECO:0000313|EMBL:AAV45174.1, ECO:0000313|Proteomes:UP000001169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:AAV45174.1}, and ATCC 43049 / DSM
RC 3752 / JCM 8966 / VKM B-1809 {ECO:0000313|Proteomes:UP000001169};
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [2] {ECO:0000313|EMBL:QCP92959.1, ECO:0000313|Proteomes:UP000298722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:QCP92959.1,
RC ECO:0000313|Proteomes:UP000298722};
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; AY596297; AAV45174.1; -; Genomic_DNA.
DR EMBL; CP039138; QCP92959.1; -; Genomic_DNA.
DR RefSeq; WP_011222818.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V5M8; -.
DR STRING; 272569.rrnAC0098; -.
DR PaxDb; 272569-rrnAC0098; -.
DR EnsemblBacteria; AAV45174; AAV45174; rrnAC0098.
DR GeneID; 40154409; -.
DR KEGG; hma:rrnAC0098; -.
DR PATRIC; fig|272569.17.peg.902; -.
DR eggNOG; arCOG00856; Archaea.
DR HOGENOM; CLU_000022_59_5_2; -.
DR Proteomes; UP000001169; Chromosome I.
DR Proteomes; UP000298722; 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; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43859; ACYL-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR43859:SF4; BUTANOATE--COA LIGASE AAE1; 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:0000313|EMBL:AAV45174.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001169}.
FT DOMAIN 14..384
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 437..512
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 533 AA; 59826 MW; 7FF89555D8B14284 CRC64;
MKREMLTTDF IDRAADIYDD VTGIVAHDGT EYTYAEVNER VNQLAHALSD RGVSKGSRVA
LLAPNTHYFI ETLYATNKLG AVFVPLNYRL DPAKIEYILN DCEAATVIAD YDFAEKVQPV
RDDIPAETFI GYEPDRIDGE WEAYSGILDG QPTAEPDRPE MAEDDDASIN YTSGTTGDPK
GVVRTHRTES WHSLVLNQHM EIRDDDTYLW TLPMFHCNGW GHTYAITGTG GTHVCQRTFD
AADTFRRVRE YDVSFMCGAP TVLNKLIQHY RANDGDVVTQ GDRDVRIATA GSAPATATIE
RVEDEFGWRI IHIYGLTETA PIITTSNSPR RIAERGRELK VKQGSETLCT DIRIVDEDGT
DVPRDGATIG EVVVQGNQVM DRYLNKPEIT EEAFNDRAEG YFHTGDLAAW DEDGMIQIMD
RRKDIIISGG ENISSIELED ELYDHPGVLK AAVIPTPSED WGETPMAIVV PTADSDATEQ
DILEFLRERV ASYKVPAGID FRDSLPETAT GKIQKYELRE EYWQEQERMI GQE
//
