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FABZ_FUSNN
ID   FABZ_FUSNN              Reviewed;         141 AA.
AC   Q8R690;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ {ECO:0000255|HAMAP-Rule:MF_00406};
DE            EC=4.2.1.59 {ECO:0000255|HAMAP-Rule:MF_00406};
DE   AltName: Full=(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase {ECO:0000255|HAMAP-Rule:MF_00406};
DE            Short=(3R)-hydroxymyristoyl-ACP dehydrase {ECO:0000255|HAMAP-Rule:MF_00406};
DE   AltName: Full=Beta-hydroxyacyl-ACP dehydratase {ECO:0000255|HAMAP-Rule:MF_00406};
GN   Name=fabZ {ECO:0000255|HAMAP-Rule:MF_00406}; OrderedLocusNames=FN0594;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
CC   -!- FUNCTION: Involved in unsaturated fatty acids biosynthesis. Catalyzes
CC       the dehydration of short chain beta-hydroxyacyl-ACPs and long chain
CC       saturated and unsaturated beta-hydroxyacyl-ACPs. {ECO:0000255|HAMAP-
CC       Rule:MF_00406}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00406};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00406}.
CC   -!- SIMILARITY: Belongs to the thioester dehydratase family. FabZ
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00406}.
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DR   EMBL; AE009951; AAL94790.1; -; Genomic_DNA.
DR   RefSeq; NP_603491.1; NC_003454.1.
DR   AlphaFoldDB; Q8R690; -.
DR   SMR; Q8R690; -.
DR   STRING; 190304.FN0594; -.
DR   EnsemblBacteria; AAL94790; AAL94790; FN0594.
DR   KEGG; fnu:FN0594; -.
DR   PATRIC; fig|190304.8.peg.1159; -.
DR   eggNOG; COG0764; Bacteria.
DR   HOGENOM; CLU_078912_3_0_0; -.
DR   InParanoid; Q8R690; -.
DR   OMA; FPGRPLM; -.
DR   BioCyc; FNUC190304:G1FZS-1181-MON; -.
DR   Proteomes; UP000002521; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00406; FabZ; 1.
DR   InterPro; IPR013114; FabA_FabZ.
DR   InterPro; IPR010084; FabZ.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   PANTHER; PTHR30272; PTHR30272; 1.
DR   Pfam; PF07977; FabA; 1.
DR   SUPFAM; SSF54637; SSF54637; 1.
DR   TIGRFAMs; TIGR01750; fabZ; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW   Lyase; Reference proteome.
FT   CHAIN           1..141
FT                   /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT                   FabZ"
FT                   /id="PRO_0000091680"
FT   ACT_SITE        49
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00406"
SQ   SEQUENCE   141 AA;  15951 MW;  5751F1F3A9215ED5 CRC64;
     MLDILEIMKR IPHRYPFLLV DRILEMDKEA QIIKGKKNVT MNEEFFNGHF PGHPIMPGVL
     IIEGMAQCLG VMVMENFPGK VPYFAAIENA KFKNPVKPGD TLIYDVKVDK VKRNFVKATG
     KTYVDDAVVA EASFTFVIAD M
 
 
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