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FABZ_NEIMF
ID   FABZ_NEIMF              Reviewed;         149 AA.
AC   A1KRL1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
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=NMC0170;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
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; AM421808; CAM09489.1; -; Genomic_DNA.
DR   RefSeq; WP_002216259.1; NC_008767.1.
DR   PDB; 4I83; X-ray; 2.60 A; A/B/C/D/E/F=1-149.
DR   PDBsum; 4I83; -.
DR   AlphaFoldDB; A1KRL1; -.
DR   SMR; A1KRL1; -.
DR   EnsemblBacteria; CAM09489; CAM09489; NMC0170.
DR   KEGG; nmc:NMC0170; -.
DR   HOGENOM; CLU_078912_1_0_4; -.
DR   OMA; FPGRPLM; -.
DR   OrthoDB; 1763197at2; -.
DR   Proteomes; UP000002286; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Lyase.
FT   CHAIN           1..149
FT                   /note="3-hydroxyacyl-[acyl-carrier-protein] dehydratase
FT                   FabZ"
FT                   /id="PRO_0000301905"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00406"
FT   STRAND          5..8
FT                   /evidence="ECO:0007829|PDB:4I83"
FT   HELIX           9..15
FT                   /evidence="ECO:0007829|PDB:4I83"
FT   STRAND          27..32
FT                   /evidence="ECO:0007829|PDB:4I83"
FT   TURN            33..35
FT                   /evidence="ECO:0007829|PDB:4I83"
FT   STRAND          36..42
FT                   /evidence="ECO:0007829|PDB:4I83"
FT   STRAND          45..47
FT                   /evidence="ECO:0007829|PDB:4I83"
FT   HELIX           48..51
FT                   /evidence="ECO:0007829|PDB:4I83"
FT   HELIX           62..80
FT                   /evidence="ECO:0007829|PDB:4I83"
FT   TURN            85..87
FT                   /evidence="ECO:0007829|PDB:4I83"
FT   STRAND          91..95
FT                   /evidence="ECO:0007829|PDB:4I83"
FT   STRAND          97..100
FT                   /evidence="ECO:0007829|PDB:4I83"
FT   STRAND          109..120
FT                   /evidence="ECO:0007829|PDB:4I83"
FT   STRAND          123..132
FT                   /evidence="ECO:0007829|PDB:4I83"
FT   STRAND          135..145
FT                   /evidence="ECO:0007829|PDB:4I83"
SQ   SEQUENCE   149 AA;  16613 MW;  DE6BCB39FB8DACBE CRC64;
     MDVQLPIEAK DIQKLIPHRY PFLQLDRITA FEPMKTLTAI KNVSINEPQF QGHFPDLPVM
     PGVLIIEAMA QACGTLAILS EGGRKENEFF FFAGIDEARF KRQVIPGDQL VFEVELLTSR
     RGIGKFNAVA KVDGQVAVEA IIMCAKRVV
 
 
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