ID   Q0C0M2_HYPNA            Unreviewed;       528 AA.
AC   Q0C0M2;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=2-acylglycerophosphoethanolamine acyltransferase/Acyl-[acyl-carrier-protein] synthetase {ECO:0000313|EMBL:ABI75576.1};
DE            EC=2.3.1.40 {ECO:0000313|EMBL:ABI75576.1};
DE            EC=6.2.1.20 {ECO:0000313|EMBL:ABI75576.1};
GN   Name=aas {ECO:0000313|EMBL:ABI75576.1};
GN   OrderedLocusNames=HNE_2022 {ECO:0000313|EMBL:ABI75576.1};
OS   Hyphomonas neptunium (strain ATCC 15444).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=228405 {ECO:0000313|EMBL:ABI75576.1, ECO:0000313|Proteomes:UP000001959};
RN   [1] {ECO:0000313|EMBL:ABI75576.1, ECO:0000313|Proteomes:UP000001959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15444 {ECO:0000313|EMBL:ABI75576.1,
RC   ECO:0000313|Proteomes:UP000001959};
RX   PubMed=16980487; DOI=10.1128/JB.00111-06;
RA   Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA   Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA   Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA   Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA   Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA   Ward N.L.;
RT   "Comparative genomic evidence for a close relationship between the
RT   dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT   crescentus.";
RL   J. Bacteriol. 188:6841-6850(2006).
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DR   EMBL; CP000158; ABI75576.1; -; Genomic_DNA.
DR   RefSeq; WP_011647020.1; NC_008358.1.
DR   AlphaFoldDB; Q0C0M2; -.
DR   STRING; 228405.HNE_2022; -.
DR   KEGG; hne:HNE_2022; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_59_8_5; -.
DR   Proteomes; UP000001959; 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:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:UniProtKB-EC.
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; PTHR43201; ACYL-COA SYNTHETASE; 1.
DR   PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 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   Acyltransferase {ECO:0000313|EMBL:ABI75576.1};
KW   Ligase {ECO:0000313|EMBL:ABI75576.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001959};
KW   Transferase {ECO:0000313|EMBL:ABI75576.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        75..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          34..388
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
SQ   SEQUENCE   528 AA;  56920 MW;  9274185020D0F300 CRC64;
     MQQSIQPLVP APLAYKPQRT RTDLFSALLR ASREFGGGKT IVVDGDERAL TYKEIIRAAF
     GLGSALKKGT RKGEAVAIML PTGVGAVIAF YAVSAFGRVP AMLNFTAGSK NLKAAMKAAK
     VKRIITAHKF VELGGLETLI EDLSKVAEII YLEDVRENLS LGNKLTAVAG TLLPGLVAAG
     PSHKKPAVIL FTSGTEGEPK GVVLSHENVM ANVEQVRAHI GLGPDTDVLF NPLPMFHCFG
     LTVGAILPIV AGIKVFFHPS PLQPKEIVRR ISEHKPTIML ATDTFISQYA RTAEDGDLSS
     IRLAVCGAER VKDETRAYVR RKFDIEILEG YGATEASPVV AANQWEDNRP GTVGKLMSDM
     ESRLVPVEGM PEGGKLHIRG PNIMLGYLRP SNPGVIEKLI DGWHDTGDIV TVDEDGFIRI
     MGRVKRFAKI GGEMVSLAVV ENCAAAVWPD NMHAAVTLPD PKKGEQVILL TDAPEATREP
     ILSWAKQHGV PEISVPRRVF RVAEIPVLGT GKVDYGAVGI AAERLMND
//