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Database: UniProt
Entry: E6MT97_9BACT
LinkDB: E6MT97_9BACT
Original site: E6MT97_9BACT 
ID   E6MT97_9BACT            Unreviewed;       578 AA.
AC   E6MT97;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Beta-ketoacyl synthase, C-terminal domain protein {ECO:0000313|EMBL:EFV03151.1};
DE            EC=2.3.1.41 {ECO:0000313|EMBL:EFV03151.1};
GN   Name=fabF5 {ECO:0000313|EMBL:EFV03151.1};
GN   ORFNames=HMPREF9420_2715 {ECO:0000313|EMBL:EFV03151.1};
OS   Segatella salivae DSM 15606.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=888832 {ECO:0000313|EMBL:EFV03151.1, ECO:0000313|Proteomes:UP000003874};
RN   [1] {ECO:0000313|EMBL:EFV03151.1, ECO:0000313|Proteomes:UP000003874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15606 {ECO:0000313|EMBL:EFV03151.1,
RC   ECO:0000313|Proteomes:UP000003874};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC       ECO:0000256|RuleBase:RU003694}.
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:EFV03151.1}.
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DR   EMBL; AEQO01000205; EFV03151.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6MT97; -.
DR   STRING; 888832.HMPREF9420_2715; -.
DR   eggNOG; COG0304; Bacteria.
DR   HOGENOM; CLU_467582_0_0_10; -.
DR   Proteomes; UP000003874; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR11712:SF320; BETA-KETOACYL SYNTHASE; 1.
DR   PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:EFV03151.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003874};
KW   Transferase {ECO:0000256|RuleBase:RU003694, ECO:0000313|EMBL:EFV03151.1}.
FT   DOMAIN          1..369
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   578 AA;  63634 MW;  A4E87FA337A0AF16 CRC64;
     MSAKMNQNTM VNVLADNIIS PLGETSEETY LAVKRGESAL HTYAPMTEHI PHGFVASLLS
     SDFEELLLRS TQSAVNASGV DVKNTRTVFI LSSTKGEIEK LGKTADETLY LGNVAQRIAT
     RLGIKQTPIV VCNACISGLA AIVLASRLLS SNTYDYAVVC GADRPRRFII SGFQSLNAMS
     AFSCQPFDIE RQGLNLGEAY ATIVLARETK ASLHTNSHVW QIGHGYVKND AYHISAPSKT
     AEGLVEALQA TMEGVDTEEL AFINAHGTAT LFNDQMEAIA IQRTGLQHIP VNALKGYIGH
     TLGAAGIIET ILCMKSVDDH LILGTRGFEE VGVSGKVKLS STHQTTQKKA FLKLLSGFGG
     CNATLFARSV ESDEASNVCV DETTKLPSHV EMKHHVRLSP QGVWLNDKVF AVDERETQHN
     LLTAIYKQQI GNYPKYYKMD GLCRLGFVAS ELLLQAEREE GPCKEDVNKA RAIVFFNRSS
     SIVSDKKYLT SIADKDNYFP SPSVFVYTLP NIVTGEIAIR NGYHGETSFY ILPKKNELLM
     QHIIESAFMD DQTTSMITGW LDYEDDKHFE ADLYIAYK
//
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