ID C7CM15_METED Unreviewed; 1138 AA.
AC C7CM15;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Bifunctional protein (Aas-like): 2-acylglycerophosphoethanolamine acyltransferase and Acyl-acyl carrier protein synthetase {ECO:0000313|EMBL:CAX23764.1};
DE EC=2.3.1.40 {ECO:0000313|EMBL:CAX23764.1};
DE EC=6.2.1.20 {ECO:0000313|EMBL:CAX23764.1};
GN ORFNames=METD_I2163 {ECO:0000313|EMBL:CAX23764.1};
OS Methylorubrum extorquens (strain DSM 6343 / CIP 106787 / DM4)
OS (Methylobacterium extorquens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=661410 {ECO:0000313|EMBL:CAX23764.1, ECO:0000313|Proteomes:UP000008070};
RN [1] {ECO:0000313|Proteomes:UP000008070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6343 / CIP 106787 / DM4
RC {ECO:0000313|Proteomes:UP000008070};
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
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DR EMBL; FP103042; CAX23764.1; -; Genomic_DNA.
DR RefSeq; WP_015822116.1; NC_012988.1.
DR AlphaFoldDB; C7CM15; -.
DR GeneID; 72989157; -.
DR KEGG; mdi:METDI2163; -.
DR HOGENOM; CLU_008489_1_0_5; -.
DR Proteomes; UP000008070; 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; ACYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43201:SF5; MEDIUM-CHAIN ACYL-COA LIGASE ACSF2, MITOCHONDRIAL; 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:CAX23764.1};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000313|EMBL:CAX23764.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000313|EMBL:CAX23764.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 52..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..421
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 835..856
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 455..565
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 1138 AA; 121152 MW; 69F069DBA4BCA305 CRC64;
MFRTLMTTRR FAPLFWCQFF SAFNDNFLKN ALALLILFQV SARGESSGGV LVTLASAVFI
GPFFILSGLG GQMADRYDKA VLAKRLKFAE IFAALLSVLG FWLHSVPLLF AALGLFGIIA
ALFGPIKYGI LPDHLKREEL TAGNALVEAA TFLAILLGTI TAGLAMAMGG HALGLGAGLM
GMAVLCWLAA RMIPATGEGA PDLHVDRNVA RSTAELLRDL WSDTRLWRGS VIVSWFWLVG
VVILSLMPVL VRQTLNGTEI VATTLLAIFS VGIAVGSGLA SWLASGRIVL LPTPVGAVLM
GLFGLDLAWT VSQVSPAIGE PVGAWDFISG GSGLRIAIDF FGLAVAGGLY VVPSFAAVQA
WTEKAKRARV IGAVNVLTAA FMVAGTLALA VLQGLGLSTA QLLGLVAVLN LIAGAVILVT
LPTNPLRDAL SILFRAFYRL EVKGLENVEK AGPNAIVALN HVSFLDAPLA LSLLDKEPVF
AIDHGIAQRW WVKPFLKVTK AMPLDPTRPL ATRTLINAVK SGETLIIFPE GRLTVTGSLM
KVYDGAGLIA DKSGAMVVPV KIDGPERTIF SRLKRDQVRR AWWPKVTVTI MPPVRLHVDP
ELKGKNRRRA AGAALYDIMS DLVFETADID RGVFAALIEA GQLHGWRRTA LEDPVSGTMS
YARLVMGANI LGRKLQALLP DAKKPVGLML PNANGAAVTF FALASAGRVP AMINFSAGPA
AVLSACRAAQ VDTLLTSRAF IEKGRLGALI EGIQGSLRLI YLEDVRAGVT TGDKIRGFLE
PRRPLVARHG SDPAAILFTS GSEGTPKGVM LANRAMLANT AQVAARIDFG PRDKVFNVLP
VFHAFGLTAG LVLPLISGVP VYLYPSPLHY RIVPELIYGT NATVLFGTDT FLTGYAKMAH
SYDLRSLRYV VAGAEPVKQA TRKTWAEKFG LRILEGYGVT ECGPVLALNT PMFNRFGTVG
RLLPGIESRL EPVPGIDEGG RLMVRGPNIM LGYLRAENPG VLEPPADGWY DTGDIVAFDA
DGFVTIKGRA KRFAKIAGEM VSLASVEALA AELWPDAPSA VAAVPDARKG ERLILFTQAK
GATRAAYQTH AKSRGAADVA VPAEVVVLEG LPMLGTGKVD QVSVTKLARE RAATAEAA
//
