UniProt: W7P0L9

Database: UniProt
Entry: W7P0L9_9ENTR

LinkDB:  W7P0L9_9ENTR 
Original site:  W7P0L9_9ENTR

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (44)   
   InterPro (26)   
   Pfam (8)   
   PROSITE (6)   
   SMART (4)   
Literature (1)   
   PubMed (1)   
All databases (54)   

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ID   W7P0L9_9ENTR            Unreviewed;      2578 AA.
AC   W7P0L9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000313|EMBL:EWG74982.1};
DE            EC=5.4.3.8 {ECO:0000313|EMBL:EWG74982.1};
GN   Name=hemL_2 {ECO:0000313|EMBL:EWG74982.1};
GN   ORFNames=P349_02347 {ECO:0000313|EMBL:EWG74982.1};
OS   Enterobacter sp. DC4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=1395580 {ECO:0000313|EMBL:EWG74982.1, ECO:0000313|Proteomes:UP000019283};
RN   [1] {ECO:0000313|EMBL:EWG74982.1, ECO:0000313|Proteomes:UP000019283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DC4 {ECO:0000313|EMBL:EWG74982.1};
RX   PubMed=24625871;
RA   Gan H.M., Triassi A.J., Wheatley M.S., Savka M.A., Hudson A.O.;
RT   "High-Quality Draft Whole-Genome Sequences of Three Strains of Enterobacter
RT   Isolated from Jamaican Dioscorea cayenensis (Yellow Yam).";
RL   Genome Announc. 2:e00170-14(2014).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|ARBA:ARBA00008467}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EWG74982.1}.
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DR   EMBL; AZUB01000003; EWG74982.1; -; Genomic_DNA.
DR   PATRIC; fig|1395580.4.peg.2332; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000019283; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05931; FAAL; 1.
DR   CDD; cd00610; OAT_like; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
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; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR040097; FAAL/FAAC.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Isomerase {ECO:0000313|EMBL:EWG74982.1};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          575..656
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          667..1079
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1529..1607
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2578 AA;  278457 MW;  5D35C545E25AE9E9 CRC64;
     MMPSHQLFNR GYHSFNQLLP ELAVQQTTQT AFEFVRSASE IHSQSYDQLH QRAASLAEAL
     MQYGQRGDRV ILLYPDGEDF IGAFFGCLYA GRVAVPVPMP AKSSGSAWER FAGVLHNAQT
     DCIVTTARGA ETLGQLSLPL SPLIFTFDKP DTSALPAGYR LHHLERTFSG AFHPVPVADN
     DLAFLQYTSG STGSPKGVMV THGNLWANSH AIHRFFGHHS ESRGMIWLPH FHDMGLIGGL
     LQPVFGAFPC RVMSPMMLMK NPLNWLKQIS DYQATTSGGP NFAYELCVRK IGREQVEALD
     LSRWDVAFCG AEPIRPATLA QFSEHFAPAG FRPGAFLPCY GMAETTLIVT GMDKGQGLRV
     SYEAGAVSCG QALTDTEVRI VDPDHHQPLA DGESGEIWLR GPSVAAGYWA NDAATRETFR
     ASLAGDPHPW LRSGDMGFLQ SGHLYVTGRL KELLIINGQN HYPTDIEETI RQSAPALVEA
     TVCVFASEDE RPVALLELMT RHKNDLDMAT LAPSVTAAVA ERHGITLDEL LLVERRAIPR
     TTSGKLQRTR AKMMYQQGTL DVSWRSRQDA SKPVEHAGET SPALAALIAG IIGNTLNTTI
     GESRWDDAFT GFGLSSLQAV GVIGELEQRL GRELSPALIY DYPTINQLAV ALGEPAAVRP
     VSAAVAESAI AVIGIGVELP GHSGVEALWS LLQQGHSTTG EIPAQRWRTS SLDGFNRKGS
     FFDEVDAFDA GYFGISPREA VYIDPQHRLL LETVQQAFTD AGLKASSLRG SDTAVYVGIS
     ASDYALACGD NVSAYSGLGN AHSIAANRIS YLYDLKGPSV AVDTACSSSL VAIEGAMQSL
     RAGRSSLAIA GGVNLALTPH LQKVFTDAQM LAPDGRCKTF DARADGYVRG EGCGVVVLKP
     LSQALADGDR VYATLVASAV NQDGRSNGIT APNGPSQQAV IRQAMADAGV DSDSIDYIEA
     HGTGTALGDL IEYQALEAVF ADRKKNAPVQ VGSIKTNIGH LEAAAGVLGV VKTSLMLHYR
     QYVPHLNFQH KNPHIAAISR HVEVSGAQPA SWHADGDARY AGVSSFGFGG TNGHVILRSA
     PAVEKRQEPA APHGLLLIGS HDEGAFTLQR EAVKKGLSTC QDSDIATWCR LVNTRYDAAR
     YRGVAYGADR AQLADSLAQL TACKAGKAQP QVWLFPGQGT QQIGMGAELY HHLLHYRTQF
     DALATTIRQR YQIDITQALF ARDDSWQRCA RTCQLSLFAC SYALAQSMMQ FGPRPAAVMG
     HSLGEYCAAV IAGYLSLDDG LAMVHQRALL MSALTQEGAM AVVFSGEAEV CQLISPWAGD
     IDIAAFNTPT LTTIAGSQTA IDACLQTISA QGGHARKIKT ASAFHSSMMD PILGAWREWL
     VNNVTFTRGT IPFYSNLNGE VCDQTDADYW TRQIRQPVRF LQGVQNVLAQ GEFTFIDLSA
     DSSLGKFVTA TDRRHRVLAA GDRRHEYKSL LTLLGTLWQH GHDINWSGLY HATTREALNL
     PAIQFCRKRY WLADETPAQT PSAKEDAMSN QHHLAAEIKA IIAGFLEADP ATLDDELPFL
     EMGADSLVLL DAINTIKDRY GVAIPVRALF EELNTLDAVI GYVVEHAQPA AAVPPSATET
     AEQAAQPVVA MPETSKPVPG AVQDLIARQL ELMSQQLTLL NGAAQTLPMP VAPTMSDVIA
     PAPIATPAAP VKASAHSSWF KKETKKVSLG TERDQHLAQL TQRFVDKTGG SKRNAQQYRA
     VLADNRASAG FRLSTKEMLY PLVGERSQGS RIWDVDGNEY IDFTMGFGAN LLGHAPDCVQ
     QAVADQLARG MQIGPQSALA GEVATLISEL TGQQRVAFCN SGSEAVMSAV RLARAVTGKN
     KVALFSGSYH GVFDGILGRQ QGGETPERAT PIAAGTPPSL VDDLLVLDYG SEESLALIAR
     YAAELAVVIV EPVQSRYPDH QPREYLHTLR ELTTTHNIAL MFDEVITGFR LAAGGAQAYY
     GVQADIASYG KIVGGGMPIG VIAGSARFMD SIDGGFWQYG DDSWPQAELI FFAGTFSKHP
     LTMAASKAVL EYIKAHPALY DDINQKTARL TMSLNNWFSA TGTPIEIVSA GSLFRFKFNG
     NYDILFHHLM LRGIFIWEGR NCFVSVAHTD EDIDRFIAAV KESVNAMRVD GFFGQAGLRP
     DTRYAVADSQ QRFLQLAARD ESGRLAGTIG GVIETPRNVD SEIMLAAWQL LCERHDALRM
     QFTDAGELQV ALAPTVDISE EYAAPAACLA EFAARPFDLT AAPLARLLLV RHEGKTTLAI
     AAHHSVADGW SFMVMLRELL HLYDALASGK RPDLAAAASY LQAIRAQNIV SEAALPARLA
     ALPARRATPD VLTVMAPSRT YQGQRLVQRL SYPGLTAQLR KASAELRVTR FAMLNALFTL
     TLEKAVGHSP VPVGVPDAGR DFGQGDALVG QCVRLLPLCI DSAACASLSD VARAIHDGIL
     AQRDERALPS RCFHGQDAPI PLLATFNVEP HAPLAELRQW EASLSLLPIG AVEFPLMVNI
     LETKEGLSVE LDYQMRYFTE ASARALLEHF LKAIAVLAEQ GEEAAEALFS SSEVLAAS
//

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