ID   A0A2X0V7P0_9GAMM        Unreviewed;      1163 AA.
AC   A0A2X0V7P0;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Bifunctional protein aas {ECO:0000313|EMBL:SPT70379.1};
GN   Name=aas {ECO:0000313|EMBL:SPT70379.1};
GN   ORFNames=NCTC13093_01794 {ECO:0000313|EMBL:SPT70379.1};
OS   Anaerobiospirillum thomasii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Succinivibrionaceae; Anaerobiospirillum.
OX   NCBI_TaxID=179995 {ECO:0000313|EMBL:SPT70379.1, ECO:0000313|Proteomes:UP000250086};
RN   [1] {ECO:0000313|EMBL:SPT70379.1, ECO:0000313|Proteomes:UP000250086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13093 {ECO:0000313|EMBL:SPT70379.1,
RC   ECO:0000313|Proteomes:UP000250086};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; UAPV01000001; SPT70379.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2X0V7P0; -.
DR   Proteomes; UP000250086; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; PTHR24096:SF149; 4-COUMARATE--COA LIGASE 1-RELATED; 1.
DR   PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000250086};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        44..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        81..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        240..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        275..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        306..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        331..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        371..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        396..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          449..563
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   1163 AA;  128209 MW;  29F19DA969E3848F CRC64;
     MGSKVGTKVI LAFSLVAFIN AFVDLGHKIN IQNTLYKVYD GSTLTYMTAI VNALILLPFI
     MLMTPAGFLS DRFNKNKIMR TSAAFSVLIT IAICICYYYG QFMLAFAATF IMALQSALYS
     PAKYGYIKDL MGKDGLTFGN SLMQGIAIVA ILSGMTVFSY IFEHLYADAN LVSPDSAEIL
     KSIMPSGLIL VGMAICEYLC TLMLPDVTQD RQSLNFDFKR YIKGSLLKEN MALLKSNDKI
     IMSVIAVSIF FAVSQMLLAA FPTYIKQTFN ELNTFYVQLV LGASGLGIIA GSYITLKLSP
     HYIETGLIPL GAIGITICST LLMAFDSLVS YSILFFVFGL TFSLVIIPLN SLMQFYAPDE
     ALGKVLSGNN FIQNLAMLLF LIIAATVSLY EIDVSYLFYL SMITLTLGCI YILKKLPFSL
     ARGFVAIIFR QRYRLNIEGF NHIPSDGGVL LLGNHVSFID WAILQLALPR KVFFVIDRVF
     YEKWYLNFIL KLFGVIPVSS GGSKKALKAI ADKIKEGHMV CLFPEGCLSR HGHLNAFKKG
     FEMALKDLDV KDGVIIPFYI RGLWGSAFSR SHQAFIERQQ RLNKRSVSIA FGRAMDIHSS
     ASAVKAQVFE LSLKAFKNQC EKLSVIGSAF IDTAKKYKHK TAIVDSKSGS ISYIKMLTVC
     LLILKNYKQE LKDQRRIGIL LPASLASSVL NMTMLIMSKV VVNLNFTASN DVLASCVKRS
     QIKTIFTSRQ FLQKLEKRGI VFDFGPEVKQ VFAEDLFSSL KGQKSAYLFT SLMTRVLPAF
     LLKLLYIKNR QNSKTAAILF SSGSEGEPKG VMLSHMNIMS NIKQISDVLQ PRDSETILSS
     LPPFHAFGLT VTSLLPLVEG IKSVTHADPT DAQGIARAVV QNEVSIMCGT STFLGIYARS
     PKIAPVMFES LRVVVAGAEK LKSDVKQAFE LKFKKDILEG YGATETTPVV SVNLPDGLDR
     EFLEVHKGSK EGSVGMPLPG STVRVVDPDT LQELECGEDG LILIGGHQVM KGYLNDKERT
     DSVIASIDGI RWYKSGDKGH LDADGFLHIV DRYSRFAKIG GEMISLSALE NEIGSIISAE
     GYDSSCRFVA INIDDSKKGE KIVLLISHVE DLKPLQSLLN EKIKNALSRP SKIIKVNEVP
     LLGSGKVDFA KARAMALCDG LTN
//