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Database: UniProt
Entry: Q487U9_COLP3
LinkDB: Q487U9_COLP3
Original site: Q487U9_COLP3 
ID   Q487U9_COLP3            Unreviewed;       631 AA.
AC   Q487U9;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Acid-CoA ligase family protein {ECO:0000313|EMBL:AAZ27391.1};
GN   OrderedLocusNames=CPS_0917 {ECO:0000313|EMBL:AAZ27391.1};
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ27391.1, ECO:0000313|Proteomes:UP000000547};
RN   [1] {ECO:0000313|EMBL:AAZ27391.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=34H {ECO:0000313|EMBL:AAZ27391.1};
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; CP000083; AAZ27391.1; -; Genomic_DNA.
DR   RefSeq; WP_011041760.1; NC_003910.7.
DR   AlphaFoldDB; Q487U9; -.
DR   STRING; 167879.CPS_0917; -.
DR   KEGG; cps:CPS_0917; -.
DR   eggNOG; COG0365; Bacteria.
DR   HOGENOM; CLU_000022_3_6_6; -.
DR   Proteomes; UP000000547; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd05967; PrpE; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR032387; ACAS_N.
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; PTHR43347; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43347:SF3; ACYL-COA SYNTHETASE SHORT-CHAIN FAMILY MEMBER 3, MITOCHONDRIAL; 1.
DR   Pfam; PF16177; ACAS_N; 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:AAZ27391.1}.
FT   DOMAIN          9..56
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          66..447
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          512..591
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   631 AA;  69072 MW;  AB24854C0E10E728 CRC64;
     MKHIEQQELA INSPESYWKE QSELVAWYKK PQTILSTNTD SWHDWFADGE LNSCYLALDY
     HVEQGRGAQT ALIYDSPVTG KKQKFSYLEL TSLVAKFADV LRSQDVTKGD RVLIYMPMIP
     QAAIAMLACA RLGAIHSVVF GGFAANELAV RINDAEPKVI VGASCGVEIA KVIPYKPLID
     QAIEIANHKP KNCIIYQREE VQAQLVPNRD LDWQEQMDVA VEIPAVPVKS TDPLYILYTS
     GTTGKPKGVV RDNGGHAVAM LYSMKNIYGM QKGDTFWAAS DVGWVVGHSY IIYGTLMAGC
     TTIVYEGKPI RTPDAGAFWR VCAEYKVNAL FSAPTAFRAI GKEDPEGDLL KDYDLSSLKR
     LFLAGERLDP ATYHWLKEKT QLPVIDHWWQ TETGWAIAST PLDDGSDNIV ATKAGSAGFP
     IAGFDVQILD GDGQQVPAGQ QGSVAIKLPL PPGCLATIYR DSERLVSGYL SNHPGYYTSG
     DGGYIDEEGY LFIMGRIDDV INVAGHRLST GEMEEVLSGH PAVAECAVVG IHDALKGQVP
     LGLVVIKNGI TTSDEDLISE LKQSIRNDIG AIASLKKLLI IDRLPKTRSG KILRKTLRQM
     IDGQEIEIPS TIEDSQVITE LSGALVGINK D
//
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