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Database: UniProt
Entry: A0A1I2QC29_9CORY
LinkDB: A0A1I2QC29_9CORY
Original site: A0A1I2QC29_9CORY 
ID   A0A1I2QC29_9CORY        Unreviewed;      3039 AA.
AC   A0A1I2QC29;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Fatty acid synthase, bacterial type {ECO:0000313|EMBL:SFG25858.1};
GN   ORFNames=SAMN05660282_00384 {ECO:0000313|EMBL:SFG25858.1};
OS   Corynebacterium spheniscorum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=185761 {ECO:0000313|EMBL:SFG25858.1, ECO:0000313|Proteomes:UP000199065};
RN   [1] {ECO:0000313|EMBL:SFG25858.1, ECO:0000313|Proteomes:UP000199065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J11, PG 39 {ECO:0000313|Proteomes:UP000199065};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|ARBA:ARBA00005254}.
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DR   EMBL; FOPJ01000002; SFG25858.1; -; Genomic_DNA.
DR   STRING; 185761.SAMN05660282_00384; -.
DR   Proteomes; UP000199065; Unassembled WGS sequence.
DR   GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; 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:0008897; F:holo-[acyl-carrier-protein] 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; cd08950; KR_fFAS_SDR_c_like; 1.
DR   Gene3D; 1.20.930.70; -; 1.
DR   Gene3D; 3.30.70.2430; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.90.25.70; -; 1.
DR   Gene3D; 6.10.140.1400; -; 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; IPR040899; Fas_alpha_ACP.
DR   InterPro; IPR047224; FAS_alpha_su_C.
DR   InterPro; IPR003965; Fatty_acid_synthase.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
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; 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; PF18325; Fas_alpha_ACP; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF01575; MaoC_dehydratas; 1.
DR   PRINTS; PR01483; FASYNTHASE.
DR   SMART; SM00827; PKS_AT; 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; PS00606; KS3_1; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199065}.
FT   DOMAIN          2494..2949
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   REGION          1148..1170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1154..1170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3039 AA;  323495 MW;  85BDADC6F50DB2CA CRC64;
     MSDQHKALNP EQPRLNQRLL EEGAGFALAY AGQGQPWLST LADNLHASTE VHDAVAMAVK
     GANAMVQPVA DELAAARPEG FKPVAWAEER IDAPTDEYQP AYSVPGITVA QMAVTYALRA
     QGLPTEAAKA VIAHSQGVLA AYPMQGRCDD ATAIALAELI GVAMTRQGRI SGLIAGNGAA
     GISPMVAIGG VSKDIVEYAI AKAKVSSVVG LVNSREDVVM VGRPADNATV IRLLKAQSAK
     EQKELDDKRR GGTALNPRFT QLEVRAGFHH PDMQAGADQV VQWAERCGID IELARDAAQA
     VMVTPVDWPR EIAAVVDAGA TWVLDLGPGR GVQSLTAKIL RGRGVGSLAV ADSEGQADLF
     DAGRKLKEPL DYSEYLPKVV DVHGQKRLRT KFTELTGQSP MLLAGMTPTT VDAEIVAAAA
     NSGHWAELAG GGQVRQNILE RSIEKLSGLL DEGVSASFNA MFLDPKLWGL HIGGRKLVQK
     ARQAGAPIDS IVVSAGMPEP EEAELLLAEL EANGFNHVAF KPGAVNQIRR VLALADRVPE
     TPIIMQVEGG KAGGHHSWED LDDLLIATYE DIRRRPNVVL CVGGGIGTPE RAADYLTGQW
     AKPYALPLMP VDGILIGTAA MAAKEAKTSP QVKRALVEAQ GDPNAWVPAG RAVHGVASGR
     SQLGADIHEI ENSFAKAGRL LDEVAGDAEA VAKRREEIIA AINKTCKPYF GDVQTMSYAQ
     LIRRYLELSG PYDAEAAAAV ELPEEDHGWV NRAWFTRFAE LIERTEARLS PVDSGEFDAQ
     VETRIDKDPQ ETLQELLAAY PAAEDQVLHP ADVDWFYALC VSSGKPVNFV PVIDKDVRRR
     WRSDSLWQAH DPRYEADEVC IIPGPAAVAG ITKMDEPIAE LLGRFDQASI ERILESGAEV
     SEDRTPVIRQ ILNARTTEWA GRQQRSLIHR LGAPETWEEK GEGFYHPESG ATLESSASGA
     MLNVPLTDGE LKVPYRLSAG APGGVVPTVS AHDAEESMAA LTKVAAGGQL AEANGLKAHW
     ETQIQAAKLA DYATVTTGHL GSNTVHVDAD QLTPDVLVGY AWPAIFSAVR ASGAVEGMLS
     LVHLDHQIAV EEDLDGLSDG ITLVIDAEAQ EPVDTEMGRV VMVKATINAR HKTIATLKER
     FLVRGRTGTD PMPQWADEAT SENTATDTPR SFRAATTVQA PRSMRSFAIV SGDRNPIHVD
     QAAAALAGLG EPIVHGMWTS AIAQIVAAAG YEGEETTTAP GVVKEWSASM IAPVLPGATV
     DIQVDRIGVD SRPGYGEIRN VTATVDGQPV LSATATMAAP VTFYAFPGQG IQSQGMGMAS
     RASSAAARAV WDRADKHTRE KLGFSVLHIV QDNPQDVWVD GEKFSHPDGV LYLTQFTQVA
     MATLGVAQVA EMEEAGVMED HSYFAGHSVG EYDALSAYSG VLSLESVVEI VYRRGLTMHR
     LVERDENGLS TYGLAALRPN KMGLSEDEVF DYVTEMSEKC GEFLEIVNYN IAGVQYAVAG
     TVKGLSAMQA DVEKRAPGQR AYIRIPGIDV PFHSSKLRDG VGDFREHLNA LLPETFNLDR
     LIGRYIPNLV ARPFELSYEF VESMTEVVDS EIINGILENF EEASKDEHVL ARTILVELLA
     WQFASPVRWI ETQALALEDL GVQRFIEVGV GDSPTIANMM GQTLRLPRYA GHPIEVLNVE
     RDRPVVFASD EISRALPEVD AEAEGTDVQA SVSAADSSTA EASAAAPAAA PAAATTAPAA
     SAPAATGGAR PDDLLLSAGE ATEMLIAVWT KVRPDQMTPT DSIETLVEGV SSRRNQLLLD
     LGVEFGLGAI DGAADAALED LKAQVAGLAR GYKAFGPVLG EASADALRRL TGPTGKKPTY
     IRERVTGTWE LGEGWADQVT AALVLGTREG ASLRGGELAT LQPANPSKAA DLDELIDAAV
     QAVAAQHGVS VSLPSAGGGA GGAVVDSAAL NEFAENLTGK DGILAQTARD LLERLGLQDQ
     ADALVDAGAD DRAIVALVER ELGADWPKQV APSFNPDKAV LLDDRWASAR EDLSRAVLNS
     TTDDLDLHGA GEAVAAQAEY LGYPELAAQA RNEEPLRYSA DTAVVTGGSP NSIAASIIAQ
     LLHGGATVVA TTSSLNHKRL EFYKKLYANN ARGNAALWVA PANLSSYEDL DNLVEWIGNE
     QTATVNGAKK VLKKPLIPTL LFPFAAPGVS GSVDDAGPQA ESQMRLLLWS VERLVAGLSH
     IGSDVSVGHR LHVVLPGSPN RGRFGGDGAY GESKAALDAL VTRWKAEQPG WGERTSLVHA
     HIGWIRGTGL MGHNDVLVDE VEKAGVRTFS TEEITEKLLS QATPEVRNQA AQAPITVDYT
     GGLAEAELNL PELARTAREK AEASDAAEAS TTTPRTIAAL PSIRQPLQWT NPTFQPVQRS
     LDDMVVMVGV GELSPLGSSR TRFEVELGDT LSAAGVTELA WSMGLISYED GAWRDSDGEE
     VPETEIRERY LDEVMAKIGV RQFHDDFHMV DNLAPELTQV YLDRDLTFAA ADEAEARSFL
     EAEPDTTRIA FDGDTEEWLV TRTAGAAVRV PRRVVMTRFV GGQIPEGFDP AVWGIPADMI
     DNLDRVAVWN LVCTVDAFLS SGFSPADILG AVHPGRVSST QGTGMGGVQS MRSLYIDGLL
     AEPRANDILQ EALPNVVAAH VMQSYVGGYG QMIHPVAACA TAAVSVEEGS DKIRLGKADF
     VVAGGIDDLS IEGITGFGDM AATADSAEMR AKGIDDRYFS RANDRRRGGF IESEGGGTVL
     LARGSFAADY NLPVLAVVGY AESFADGAHT SIPAPGLGAL GAARGGQHSG LGRSLAALGL
     NADDIAVISK HDTSTTANDP NESDLHERIA GALGRSDGNP LYVISQKTIT GHAKGGAAAF
     QLGGLAQVLR CGTIPANRSL DCVDPVLRKH QHLVWLRQPL ALSGALTPKA GLVTSLGFGH
     VSALIMLAHP GVFLTALAQE RGCEAAEAWQ AAARGKEYRG LQLILGGMHQ VNPLYQRPQD
     RHLGGTDDAA KEREAAVLLD DRARLVDGIL TIPEEEEQA
//
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