(data stored in ACNUC7421 zone)

HOGENOM: ACHLI_1_PE436

ID   ACHLI_1_PE436                        STANDARD;      PRT;   310 AA.
AC   ACHLI_1_PE436; A9NFF0;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3; EC=2.3.1
DE   180;AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III;AltName:
DE   Full=Beta-ketoacyl-ACP synthase III; Short=KAS III; (ACHLI_1.PE436).
GN   Name=fabH; OrderedLocusNames=ACL_0461;
OS   ACHOLEPLASMA LAIDLAWII PG-8A.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Acholeplasma.
OX   NCBI_TaxID=441768;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACHLI_1.PE436.
CC       Acholeplasma laidlawii PG-8A chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:FABH_ACHLI
CC   -!- FUNCTION: Catalyzes the condensation reaction of fatty acid
CC       synthesis by the addition to an acyl acceptor of two carbons from
CC       malonyl-ACP. Catalyzes the first condensation reaction which
CC       initiates fatty acid synthesis and may therefore play a role in
CC       governing the total rate of fatty acid production. Possesses both
CC       acetoacetyl-ACP synthase and acetyl transacylase activities. Its
CC       substrate specificity determines the biosynthesis of branched-
CC       chain and/or straight-chain of fatty acids (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + malonyl-[acyl-carrier-protein] =
CC       acetoacetyl-[acyl-carrier-protein] + CoA + CO(2).
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- DOMAIN: The last Arg residue of the ACP-binding site is essential
CC       for the weak association between ACP/AcpP and FabH (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the fabH family.
CC   -!- GENE_FAMILY: HOG000246674 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A9NFF0; -.
DR   EMBL; CP000896; ABX81080.1; -; Genomic_DNA.
DR   RefSeq; YP_001620456.1; NC_010163.1.
DR   ProteinModelPortal; A9NFF0; -.
DR   STRING; A9NFF0; -.
DR   GeneID; 5803120; -.
DR   GenomeReviews; CP000896_GR; ACL_0461.
DR   KEGG; acl:ACL_0461; -.
DR   OMA; VPNEVIL; -.
DR   BioCyc; ALAI441768:ACL_0461-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0033818; F:beta-ketoacyl-acyl-carrier-protein synthase III activity; IEA:EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01815; FabH; 1; -.
DR   InterPro; IPR013751; ACP_syn_III.
DR   InterPro; IPR013747; ACP_syn_III_C.
DR   InterPro; IPR004655; FabH_synth.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR016038; Thiolase-like_subgr.
DR   Gene3D; G3DSA:3.40.47.10; Thiolase-like_subgr; 2.
DR   Pfam; PF08545; ACP_syn_III; 1.
DR   Pfam; PF08541; ACP_syn_III_C; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   TIGRFAMs; TIGR00747; FabH; 1.
DR   HOGENOMDNA; ACHLI_1.PE436; -.
KW   Acyltransferase; Complete proteome; Cytoplasm;
KW   Fatty acid biosynthesis; Lipid synthesis; Multifunctional enzyme;
KW   Transferase.
SQ   SEQUENCE   310 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKNLPIKIVS TGRYAPDNIM TNDDFSKILD TNDEWITTRT GIKRRHIAQG ETAIDMAYKA
     ALKAVENKNY DKEKIDLIIV ASITSPVKTP SIANLIQAKL GLNHKNIVAF DINAACSGFV
     YAVEIAASMI SSGNYKSALV IGSEHMSSIL DWEDRSTAIL FGDAAGAAII EVSDNPKDNA
     YFWNGSRGDD TGILWIDPKV KMAGREVYKF AVDIMPKAIH KVLEKAGLTI DDIDYIIPHQ
     ANYRIIQSVA KDMNLPIERF LMNLEEYGNT SAASIPFLLD EHKTNNPEVK RVILVGFGGG
     FTWGAAILNV
//

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