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Database: UniProt
Entry: A8GFH1_SERP5
LinkDB: A8GFH1_SERP5
Original site: A8GFH1_SERP5 
ID   A8GFH1_SERP5            Unreviewed;       573 AA.
AC   A8GFH1;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, 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=Spro_2760 {ECO:0000313|EMBL:ABV41861.1};
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741 {ECO:0000313|EMBL:ABV41861.1};
RN   [1] {ECO:0000313|EMBL:ABV41861.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568 {ECO:0000313|EMBL:ABV41861.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) 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; CP000826; ABV41861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8GFH1; -.
DR   STRING; 399741.Spro_2760; -.
DR   KEGG; spe:Spro_2760; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_9_6; -.
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:ABV41861.1}.
FT   DOMAIN          40..430
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          480..554
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   573 AA;  63888 MW;  4250C52652BAEF21 CRC64;
     MIMNNDFRSN TLDKVWLKRY PADVPAEIDA DRYSSLVEMF ENAVKRYADQ PAFMNMGEVM
     TYRKLEERSR AFAAYLQNEL GLQKGDRVAL MMPNLLQYPI ALFGILRAGM VVVNVNPLYT
     PRELEHQLND SGASAIVIVS NFAHTLEKVV FNTQIKHVIL TRMGDQLSAA KGTLVNFVVK
     YIKRLVPKYH LPAAISFRSA LQRGRRLQYV KPDIINSDLA FLQYTGGTTG VAKGAMLTHR
     NMQANLEQAK AAYLPLFREG QELVVTALPL YHIFALTVNC LLFIDLGGHN LLITNPRDIP
     GLVKELGKYP FTAMSGVNTL FNALLNNEDF HKLDFSTLRF SVGGGMSVQK AVAEKWEKTT
     GKHLLEGYGL TECAPLVTGN PYDLKHYSGS IGLPVPSTDI RLVDDNGHDV PVGEPGELWV
     KGPQVMLGYW QRPDATDEVL KDGWLATGDI VTVDEMGFVR VVDRKKDMIL VSGFNVYPNE
     IEDVVSQHPK VLECAAIGVP SDVSGEAVKI CVVKKDASLT KEELLTHCRR QLTGYKVPKI
     VEFRDELPKS NVGKILRREL RDEQKKPVAA DAA
//
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