ID F4KMN1_PORAD Unreviewed; 603 AA.
AC F4KMN1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000313|EMBL:AEE12282.1};
DE EC=6.2.1.3 {ECO:0000313|EMBL:AEE12282.1};
GN OrderedLocusNames=Poras_0328 {ECO:0000313|EMBL:AEE12282.1};
OS Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC 10618 /
OS JCM 6326 / LMG 13178 / VPI 4198) (Bacteroides asaccharolyticus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=879243 {ECO:0000313|EMBL:AEE12282.1, ECO:0000313|Proteomes:UP000006545};
RN [1] {ECO:0000313|Proteomes:UP000006545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25260 / DSM 20707 / VPI 4198
RC {ECO:0000313|Proteomes:UP000006545};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I., Lu M.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Porphyromonas asaccharolytica DSM 20707.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00024484};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000256|ARBA:ARBA00024484};
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DR EMBL; CP002689; AEE12282.1; -; Genomic_DNA.
DR RefSeq; WP_013759938.1; NC_015501.1.
DR AlphaFoldDB; F4KMN1; -.
DR STRING; 879243.Poras_0328; -.
DR KEGG; pah:Poras_0328; -.
DR eggNOG; COG1022; Bacteria.
DR HOGENOM; CLU_000022_45_5_10; -.
DR OrthoDB; 9803968at2; -.
DR Proteomes; UP000006545; Chromosome.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR CDD; cd05907; VL_LC_FACS_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; PTHR43272:SF83; ACYL-COA SYNTHETASE LONG-CHAIN, ISOFORM J; 1.
DR PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:AEE12282.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006545}.
FT DOMAIN 16..429
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 603 AA; 68549 MW; 858760D01D517F9C CRC64;
MNHISDLLKL FATTYRHKTL LRYMDRTPEE QWHEWSGEQL DEQIMLAAQA LVRAGVQPGD
RVALYSQNMM EGIITELGLM AIRAVCVPLY ATCSPEQVAY ITEHAGAKLI LVGEQFQYNN
VYPLLATHPT LRQLVILDER VVRDPADDRS EYFETFLSMG DAMPYETEVR AQLGAGTPDE
TAVIIYTSGT TGTPKGVQIT HRMILTQVER HQQLFPTLND HDVSVNFLPL SHVFEKLWVY
FCLATAIKVV VVTNPKRIME LMPQIRPTVM CNVPRYWEKV YQGVQEHIER SKPMMQRIYQ
KALRVGHKYH IDYRIHGRKA PLGLRLSNAV YRYTVFYILK RVLGLERGRF FPTAGAPLSN
EINEFLQSAG FNIVVGYGLS ESSATVSCYL PGRYVIGSVG EVLPGVEVRI DPETQEIQLR
GDTITPGYYH NDEANAAAFT DDGWFRTGDA GRLEERTLYF TERIKELYKT SNGKYIAPQQ
IESLLSSSPL IEQCAVVADE RKFVAALIYP NYEQLRRRLR ERGQEALADL PTEALAQRSE
VCDLLLSHIE PLQAHLAGFE KVKRIALLAE PFSVEAGTLT PTLKLKRKAI LEQYAELIEK
LYL
//
