ID N9GGU3_ACIHA Unreviewed; 559 AA.
AC N9GGU3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 ORFNames=F927_02992 {ECO:0000313|EMBL:ENW16421.1};
OS Acinetobacter haemolyticus CIP 64.3 = MTCC 9819.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217659 {ECO:0000313|EMBL:ENW16421.1, ECO:0000313|Proteomes:UP000017667};
RN [1] {ECO:0000313|EMBL:ENW16421.1, ECO:0000313|Proteomes:UP000017667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 64.3 {ECO:0000313|EMBL:ENW16421.1,
RC ECO:0000313|Proteomes:UP000017667};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter haemolyticus CIP 64.3.";
RL Submitted (FEB-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENW16421.1}.
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DR EMBL; APQQ01000030; ENW16421.1; -; Genomic_DNA.
DR RefSeq; WP_005084046.1; NZ_KB849803.1.
DR AlphaFoldDB; N9GGU3; -.
DR PATRIC; fig|1217659.3.peg.2941; -.
DR HOGENOM; CLU_000022_59_9_6; -.
DR Proteomes; UP000017667; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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;
FT DOMAIN 31..424
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 475..549
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 559 AA; 61742 MW; 467C3C57CD9AC756 CRC64;
MEKIWFAEYQ KTGIPETVEL PAENTSLVDI FERNFQKFGS RDAFIFMDKV LTFNELEVAS
RKFATYLQSL GLAKGTRVAV MMPNVFQYPV VALGVFRAGL VLVNVNPLYT ARELEHQLND
SGSEVLVIIE NFASVYQSII GKTPVKHVVV ATVGDMLGTL KGTIVNFVLR KVRKQIPAWS
IPGHTKFNTA LNKENPSNYK RPSLTLSDTA VLQYTGGTTG VSKGAELTHR NLVGNLLQCE
AIFSSKFGAS DSEKGDRIVC ALPLYHIFAF MVCAMYGMYK GQANILIPNP RDLPAVINEL
RKYRPSFFPA VNTLFNALVN NEEFKQLDHS NLKMAMAGGM AVLPSTAEAW KKVTGTIIIE
GYGLSETSPV ATANPPATTE FSGTIGIPLP LTDVAILDDD GNELPQGEQG EISIRGPQVM
KGYWNRPDET AKVMTADGFF RTGDIGIMDT RGYFKIVDRK KDMILVSGFN VYPSEIEEVI
AQHEKVLEVA AIGVPDEKSG EVPKLFVVKK DDSLTTEEIL AFAKKNLTGY KCPRYVEFID
ELPKSNVGKI LRKDLRKPA
//
