ID A0A1X1YG31_9MYCO Unreviewed; 3080 AA.
AC A0A1X1YG31;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=3-oxoacyl-ACP synthase {ECO:0000313|EMBL:ORW10062.1};
GN ORFNames=AWC16_14620 {ECO:0000313|EMBL:ORW10062.1};
OS Mycolicibacter longobardus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=1108812 {ECO:0000313|EMBL:ORW10062.1, ECO:0000313|Proteomes:UP000193866};
RN [1] {ECO:0000313|EMBL:ORW10062.1, ECO:0000313|Proteomes:UP000193866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45394 {ECO:0000313|EMBL:ORW10062.1,
RC ECO:0000313|Proteomes:UP000193866};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|ARBA:ARBA00005254}.
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:ORW10062.1}.
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DR EMBL; LQPG01000025; ORW10062.1; -; Genomic_DNA.
DR STRING; 1108812.AWC16_14620; -.
DR OrthoDB; 4746285at2; -.
DR Proteomes; UP000193866; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00828; elong_cond_enzymes; 1.
DR CDD; cd03447; FAS_MaoC; 1.
DR CDD; cd08950; KR_fFAS_SDR_c_like; 1.
DR Gene3D; 1.20.930.70; -; 1.
DR Gene3D; 3.30.70.3320; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.25.70; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR047224; FAS_alpha_su_C.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR10982:SF23; FATTY ACID SYNTHASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF18094; DNA_pol_B_N; 1.
DR Pfam; PF08354; Fas1-AflB-like_hel; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF16073; SAT; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 2546..3001
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1732..1780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2404..2435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3039..3062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1732..1747
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3045..3060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3080 AA; 326205 MW; 4AA1FCF3070491ED CRC64;
MTIHEHDRVS ADGAGSGPFA SASSALVDRL TAGEPYAVAF GGQGSAWLES LEELVSSAGI
ETELATLAGE ADLRLEPIAK ELVVVRPIGF EPLQWVRALA VEDPIPSAKQ LTSAAVSVPG
VLLTQIAAMR ALERQGLDLS ANPPVATAGH SQGILAVESL KAGGAADVQL LAIAQLVGAA
GTLVARRRGI SILGDRPPMV SVTNADPERI HQLLEEFAQD VRTVLPPVLS IRNGRRSVVI
TGTPEQLSRF ELYCEQIAEK EAAERKNKLR GGAVFAPVFE PVQVEVGFHS PRLSDGVEIV
AGWAAKVGLD VELARQLADS ILVGQVDWVE EITTLHEAGA RWILDLGPGD ILTRLTAPVI
RGLGIGIVPV ATRGGQRNLF TIGAVPEVAR PWTSYAPSVV QLPDGRVKLD TKFTRLTGRS
PILLAGMTPT TVDAKIVAAA ANAGHWSELA GGGQVTEEIF NDRVAELTAL LEPGRTVQFN
SLFLDPYLWK LQVGGKRLVQ KARQSGAPFD GLVISAGIPE LEEAVELIAE LNEAGISHVV
FKPGTVEQIR SVIRIAAEVP TTPVIAHVEG GRAGGHHSWE DLDDLLLATY SELRSQPNIT
LCVGGGIGTP ERAAEYLSGR WSQEYGFPTM PVDGILVGTA AMATKEATTS PAVKQMLVDT
KGTDHWIGAG KAQGGMASSR SQLGADIHEI DNVASRCGRL LDEVAGDGDA VAARRDEIIA
ALALTAKPYF GDVTEMTYAQ WLRRYVELAI GAGDSTADTA SPDSPWLADT WRERFGSMLQ
RAEARLHELE SGPIETLFAD SEEGQAILER PAEAIAALLA RYPEAETVRL HPADAPFFTQ
LCKTPGKPVN FVPVIDKDVR RWWRSDSLWQ AHDARYTAEQ VCIIPGITAV AGITRVDEPV
GELLDRFEQA AIDQALAAGV QPRPVSARRQ GRTDVTGALA VLLDAPDVLW AGRTATNPVH
RIAASDEWQV HENRTATHPS TGARLEVVGD SNVVLSVPLS GVWINIRFTV PSSVVDGATP
LVSTEDAAAA MRAVLAIAAG VDGPDALPPV TNGAATVTVG WNPEQVADHT GVTATFGAPL
APGLSTVPDA LVGRCWPAVF AAIGSATTDT GFPVVEGLLS LVHLDHAAHL LAPLPAEPAE
LTVTATASAA TDTEVGRVVP VSVTVSAADG TVLATLEERF AIRGRTGAAE LTDPVRAGGA
VSDNATDTPR RRRRDVTVTA PVDMRPFAVV SGDHNPIHTD RAAALLAGLE SPIVHGMWLS
AAAQHVVTAT DGQARPPARL VGWTARFLGM VKPGDEVDFR VDRVGIDLGA EVLEVSARIG
SDLVMSATAR LTAPKTVYAF PGQGIQHKGM GMEVRARSKA ARKVWDSADK FTRETLGFSV
LHVVRDNPTS LIASGVHYQH PEGVLYLTQF TQVAMATVAA AQVAEMREQG AFVEGAIACG
HSVGEYTALA CVSGVYELEG LLEVVFHRGS KMHDIVPRDA MGRSNYRLAA IRPSQIDLDD
ADVTAFVAEI AERTGEFLQI VNFNLRGSQY AIAGTVAGLE ALEEEVERRR EITGGKRSFI
LVPGIDVPFH SEVLRIGVDD FRRSLERVMP RDKDPELIVG RYIPNLVPKP FSLDREFIQE
IRDLVPAEPL DEILADYDTW RSEKPRELCR KIVIELLAWQ FASPVRWIET QDLLFIEQAA
GGLGVERFVE IGVKSAPTVA GLATNTLKLP EYAHSTVEVL NAERDAAVLF ATDEDPEPED
EPVAEDSDAD APEGRTEPDV APAVASAGAS APSGAPRPDD IAFDAADATL ALIALSAKMR
IDQIEALDSI ESITDGASSR RNQLLVDLGS ELNLGAIDGA AEADLSGLKS QVTKLARTYK
PYGPVLSDAI NDQLRTILGP SGKRPGAIAE RVKKTWELGD GWAKHVTVEV ALGTREGSSV
RGGPLGGLHE GALADGAAVD KAIDAAVGAV AARHGVAVSL PSAGGGGGAT VDAAALGEFT
AQITGRDGVL ASAARLVLGQ LGFDDAVSAP AGATDGELID LVTAELGSDW PRLVAPAFDG
RKAVLFDDRW ASAREDLVRL WLTDEGDIDA DWPRLAERFE GAGHVVATQA TWWQGRALAS
GRQIHASLFA RIAAGAENPG RGRYSDEVAV VTGASKGSIA ASVVGQLLDG GATVIATTSR
LDDDRLGFYR NLYRDHARFG AALWVVPANM ASYADIDALV EWVGNEQSES LGPQSIHLKD
AQTPTLLFPF AAPRVAGDLS EAGSRAEMEM KVLLWAVQRL IGGLSKIGAE RDIASRLHVV
LPGSPNRGMF GGDGAYGEAK ASLDAVVARW KAETSWASRV SLAHALIGWT RGTGLMGHND
VIVDAVEEAG VTTYSTEQMA AMLLDLCNVE SKVAAANAPI EADLTGGLAE ANLDMAELAA
KAREEMTAEA SADEDSEDAA NTIAALPSPP RGYTPAPPPA WDDLDVDPAD LVVIVGGAEL
GPLGSSRTRF EMEVSGELSA AGVLELAWTT GMVKWEDDPT PGWYDTATGE LVDEAELVER
YHDAVVERVG VREFVDDGAI DPDHASPLLV SVFLDKDFSF VVSSEADARA FVEFDPEHTV
VRPVPDSSDW QVIRKAGTEI RVPRKSKLSR TVGAQIPTGF DPTVWGISQD MATSIDRVAL
WNIVATVDAF LSAGFTPTEL MRWVHPSLVA STQGTGMGGM TSMQTMYHGN LLGRSKPNDI
LQEVLPNVVA AHVVQSYVGS YGAMIHPVAA CATAAVSVEE GVDKIRLGKA ELVVTGGYDD
LTLEAIIGFG DMAATADTEM MRARGISDSK FSRANDRRRL GFVEAQGGGT ILLARGDLAA
KMGLPVLAVV AYAQSFADGV HTSIPAPGLG ALGAGRGGKD SMLARSLAKL GVGADDIAVV
SKHDTSTLAN DPNETELHER LADSLGRSDG APLFVISQKS LTGHAKGGAA VFQLMGLCQV
LRDGVIPPNR SLDCVDDELA TAGHFVWVRE TLELGEKFPL KAGLVTSLGF GHVSGLVALV
HPQAFLAALD PSQREAYLQQ ASERVLAGQR RLASAIAGGT PMYERPADRR FDHDSPEKRQ
ESAMLLNPAA RLGDGDVYIG
//
