ID B4SHV8_STRM5 Unreviewed; 558 AA.
AC B4SHV8;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|ARBA:ARBA00039545};
DE EC=6.2.1.3 {ECO:0000256|ARBA:ARBA00026121};
DE AltName: Full=Long-chain acyl-CoA synthetase {ECO:0000256|ARBA:ARBA00042773};
GN OrderedLocusNames=Smal_1831 {ECO:0000313|EMBL:ACF51535.1};
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF51535.1, ECO:0000313|Proteomes:UP000001867};
RN [1] {ECO:0000313|EMBL:ACF51535.1, ECO:0000313|Proteomes:UP000001867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3 {ECO:0000313|EMBL:ACF51535.1,
RC ECO:0000313|Proteomes:UP000001867};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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DR EMBL; CP001111; ACF51535.1; -; Genomic_DNA.
DR RefSeq; WP_012510941.1; NC_011071.1.
DR AlphaFoldDB; B4SHV8; -.
DR STRING; 391008.Smal_1831; -.
DR KEGG; smt:Smal_1831; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_9_6; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000001867; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR CDD; cd05936; FC-FACS_FadD_like; 1.
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; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43767:SF8; 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.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:ACF51535.1}.
FT DOMAIN 31..421
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 472..546
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 558 AA; 60854 MW; 494F43AA6DB0262E CRC64;
MSLDRPWLQS YPKGVPAEID VNEFHSVASV FDASVAKFRD RPAYSSFGKV ITYGETDTLV
NQFAAYLLGE LKLKKGDRVA LMMPNCLQYP VATFGVLRAG LTVVNVNPLY TARELKHQLV
DAGVSALVVV DNFGDTVEQV IADTPVKHVI TTGLGDLLGA KGAIVNFVLK YVKKMVPNYH
IKGAVRFKQA LKLGSRHTLP AVEIDHDDIA FLQYTGGTTG VAKGAMLTNR NLIANMQQAS
AWLSTSGIEP GKEVIITALP LYHIFALTAN GLVFMKFGGC NHLITNPRDM KGFVKELKGT
RFTAITGVNT LFNGLLNTPG FDEIDFSSVK FTLGGGMAVQ RAVAERWKKT TGVTLVEAYG
LTETSPAACI NPLTLPEYNG SIGLPIPSTD ACIKDDNGNI LPLGEVGELC IKGPQVMKGY
WQRPEETATA IDADGWLHTG DMARMDEQGF FYIVDRKKDM ILVSGFNVYP NEVEDVIAMM
PGVLEVAAVG VPDEKSGEVV KVVIVKKDPN LTAEMVKEHA RANLTGYKHP RIVEFRKELP
KTNVGKILRR ELRDTPAP
//
