ID F8JD87_HYPSM Unreviewed; 1147 AA.
AC F8JD87;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Putative bifunctional protein (Aas-like): 2-acylglycerophosphoethanolamine acyltransferase and Acyl-acyl carrier protein synthetase {ECO:0000313|EMBL:CCB63964.1};
DE EC=2.3.1.40 {ECO:0000313|EMBL:CCB63964.1};
DE EC=6.2.1.20 {ECO:0000313|EMBL:CCB63964.1};
GN OrderedLocusNames=HYPMC_0730 {ECO:0000313|EMBL:CCB63964.1};
OS Hyphomicrobium sp. (strain MC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=717785 {ECO:0000313|EMBL:CCB63964.1, ECO:0000313|Proteomes:UP000000494};
RN [1] {ECO:0000313|Proteomes:UP000000494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC1 {ECO:0000313|Proteomes:UP000000494};
RA Genoscope.;
RT "The complete genome of Hyphomicrobium sp. MC1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FQ859181; CCB63964.1; -; Genomic_DNA.
DR RefSeq; WP_013946374.1; NC_015717.1.
DR AlphaFoldDB; F8JD87; -.
DR STRING; 717785.HYPMC_0730; -.
DR KEGG; hmc:HYPMC_0730; -.
DR eggNOG; COG0204; Bacteria.
DR eggNOG; COG0318; Bacteria.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_008489_1_0_5; -.
DR Proteomes; UP000000494; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008779; F:acyl-[acyl-carrier-protein]-phospholipid O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR CDD; cd06173; MFS_MefA_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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 InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR43201:SF36; 2-SUCCINYLBENZOATE--COA LIGASE, CHLOROPLASTIC_PEROXISOMAL; 1.
DR PANTHER; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:CCB63964.1};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000313|EMBL:CCB63964.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000000494};
KW Transferase {ECO:0000313|EMBL:CCB63964.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 366..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 451..561
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 1147 AA; 122503 MW; 8139EC0206978BED CRC64;
MFARLLSSRR FAPLFWSQLL AALNDNLLKN ALAMLVVYKL AMENGAALGT LAGAALVLPF
FLFSALAGQL ADKFDKAKVA ARVRLIEIPI AVAAAAGFLI PSVPLLFVAL ILFGTLSAFF
GPVKYGLLPS HLEVKELPSG NALIEGATFI AILIGTVGGN FASGSHAELI AVSCAIICIS
VLGWLSARQI PPAPSSVPDL KIDRNIATST ITLLKDLRSD KRIWQGALIT SWFWLVGAGV
LALLQNLVPQ VLNGAPSVYT LALFTFAVGV AFGSVVAARA SSNRPNLALV PIGALLMGIF
LLDLAWLASR TQPAATPMTP WDVLTTLGGL HMLIDLAGIA IAGGFYIVPA FAAVQAWSPV
DHRSRVIAGC NVLSAAFMTV VGLLIAALQF EKISVATLYA GLGLANIVVV ALVLRAWGAE
GVKDVSLFLF KTFFGLEVHG RENLPKAGER AIIAPNHVSL LDAGLMHALV PSHTAYAVDT
MIAQTWWAKP FLKLTRFYTI DPTRPLGMRG LITAVKEGTS IVIFPEGRLT VTGGLMKVYD
GTAMIADKAD APIIPVRIDG LERSHFGYLS KAQTRKAWFP KTTVTILPPV WLKIDPVLRG
KARRQAAGAA LQDIMTDTAV LTTPIDQTLF EALVLAHQTR DTGKAAIEDP LGTKLTYKKL
IVGAQVLGAK IAPMLPPVGS SVGVLLPNSA GVVVTFFALQ TIGRVPAMLN FSAGPANVVS
ACKAAKVDIV LTSRVFVEKG HLEPLIKALE GVVRVVYLED IRPTITFADK VKGLMQGTRP
QVAVDYNAPA AILFTSGSEG TPKGVVLSHR NLLANCAQTL TRVACNGTDK VFNALPVFHS
FGLTAGVLMP LVAGVPIFLY PTPLHYRIIP ELVYQSNATI MFGTDTFLTG YARVAHPYDF
ARVRLVVAGA EAIKDRTRQL YMDRFGVRIL EGYGVTETAP VLALNTPLAN KAHSVGRMSP
LMDYKLEAVP GIEQGGRLYV RGPNVMLGYY RAENPGILEP PAEGWHDTGD IVEIDAQGFI
FIKGRAKRFA KVGGEMISLS AVEALAAELW PQQTTVVVAL PDQRKGERLV LLTTDAKCKR
EDFQKFARQK GTTELMVPAE ILVVSKIPLL GTGKPDYVAS LALAKEIVAA KQTTSGGAEQ
KPLTPAV
//
