(data stored in ACNUC1104 zone)

SWISSPROT: D3UZ84_XENBS

ID   D3UZ84_XENBS            Unreviewed;       728 AA.
AC   D3UZ84;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000256|HAMAP-Rule:MF_01621};
DE   Includes:
DE     RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase {ECO:0000256|HAMAP-Rule:MF_01621};
DE              EC=4.2.1.17 {ECO:0000256|HAMAP-Rule:MF_01621};
DE              EC=5.1.2.3 {ECO:0000256|HAMAP-Rule:MF_01621};
DE              EC=5.3.3.8 {ECO:0000256|HAMAP-Rule:MF_01621};
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01621};
DE              EC=1.1.1.35 {ECO:0000256|HAMAP-Rule:MF_01621};
GN   Name=fadB {ECO:0000256|HAMAP-Rule:MF_01621,
GN   ECO:0000313|EMBL:CBJ79666.1};
GN   OrderedLocusNames=XBJ1_0517 {ECO:0000313|EMBL:CBJ79666.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79666.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|Proteomes:UP000002045};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ79666.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79666.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Involved in the aerobic and anaerobic degradation of
CC       long-chain fatty acids via beta-oxidation cycle. Catalyzes the
CC       formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA.
CC       It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as
CC       substrate. {ECO:0000256|HAMAP-Rule:MF_01621,
CC       ECO:0000256|SAAS:SAAS00051718}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-hydroxybutanoyl-CoA = (3R)-hydroxybutanoyl-CoA;
CC         Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316;
CC         EC=5.1.2.3; Evidence={ECO:0000256|HAMAP-Rule:MF_01621,
CC         ECO:0000256|SAAS:SAAS01121794};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC         Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097;
CC         EC=5.3.3.8; Evidence={ECO:0000256|HAMAP-Rule:MF_01621,
CC         ECO:0000256|SAAS:SAAS01132199};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+)
CC         + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01621, ECO:0000256|SAAS:SAAS01123908};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01621, ECO:0000256|SAAS:SAAS01133165};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC         Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489;
CC         EC=5.3.3.8; Evidence={ECO:0000256|HAMAP-Rule:MF_01621,
CC         ECO:0000256|SAAS:SAAS01132197};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-hydroxyacyl-CoA = a (3E)-enoyl-CoA +
CC         H2O; Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC         ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01621, ECO:0000256|SAAS:SAAS01123900};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|HAMAP-Rule:MF_01621, ECO:0000256|SAAS:SAAS00324886}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta
CC       chains (FadA). {ECO:0000256|HAMAP-Rule:MF_01621,
CC       ECO:0000256|SAAS:SAAS00051733}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the 3-
CC       hydroxyacyl-CoA dehydrogenase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01621, ECO:0000256|SAAS:SAAS00556605}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000256|HAMAP-Rule:MF_01621,
CC       ECO:0000256|SAAS:SAAS00568097}.
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DR   EMBL; FN667741; CBJ79666.1; -; Genomic_DNA.
DR   RefSeq; WP_012987122.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0517; -.
DR   EnsemblBacteria; CBJ79666; CBJ79666; XBJ1_0517.
DR   GeneID; 8830140; -.
DR   KEGG; xbo:XBJ1_0517; -.
DR   PATRIC; fig|406818.4.peg.477; -.
DR   eggNOG; ENOG4105DYT; Bacteria.
DR   eggNOG; COG1024; LUCA.
DR   eggNOG; COG1250; LUCA.
DR   HOGENOM; HOG000261344; -.
DR   KO; K01825; -.
DR   OMA; IDLCMIL; -.
DR   BioCyc; XBOV406818:XBJ1_RS02240-MONOMER; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01621; FadB; 1.
DR   InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR012799; FadB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF48179; SSF48179; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR02437; FadB; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UZ84.
DR   SWISS-2DPAGE; D3UZ84.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00324839};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00324648, ECO:0000313|EMBL:CBJ79666.1};
KW   Lipid degradation {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00256736};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00324863};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01621, ECO:0000256|SAAS:SAAS00999128,
KW   ECO:0000313|EMBL:CBJ79666.1};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00999134};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01621, ECO:0000256|SAAS:SAAS00830857};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01621,
KW   ECO:0000256|SAAS:SAAS00324627, ECO:0000313|EMBL:CBJ79666.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   DOMAIN      316    494       3HCDH_N. {ECO:0000259|Pfam:PF02737}.
FT   DOMAIN      496    592       3HCDH. {ECO:0000259|Pfam:PF00725}.
FT   DOMAIN      628    691       3HCDH. {ECO:0000259|Pfam:PF00725}.
FT   NP_BIND     400    402       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   REGION        1    189       Enoyl-CoA hydratase/isomerase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   REGION      311    728       3-hydroxyacyl-CoA dehydrogenase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   ACT_SITE    450    450       For 3-hydroxyacyl-CoA dehydrogenase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_01621}.
FT   BINDING     296    296       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01621}.
FT   BINDING     324    324       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   BINDING     343    343       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   BINDING     407    407       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   BINDING     429    429       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   BINDING     453    453       NAD. {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   BINDING     500    500       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01621}.
FT   BINDING     660    660       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01621}.
FT   SITE        119    119       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
FT   SITE        139    139       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01621}.
SQ   SEQUENCE   728 AA;  79321 MW;  6D60FAEA5908AEC2 CRC64;
     MLYLSDTIQV NWLKDGIAEL IFNAPAAINK LDTKTVASLD KAVAVLEQQT KLKGLLLRSE
     KQAFIVGADI TEFLSLFDAP KEKLQEWLKF ANDIFSRIED LPVPTISAIN GYALGGGCEV
     VLSTDFRVAS PDLRIGLPET KLGIIPGFGG SVRLPRLIGP DNALEIITAG KDIGAEEALK
     NGLIDAVVPT EKLVDAAVSI LELAIKGDLD WQAARQPKLS PLNLNDVERT MSFTVAKGMV
     MKVAGPHYPA PITAVKTIEK AATLGRDEAL KLEAESFVPL AHTTVARALV GIFLNDQYVK
     GLAKKHLKEV TVPQHATILG AGIMGGGIAY QSARKGVPVL MKDINQKALD LGVNEAAKLL
     HKQFERGRLD AMKMAKILSS IQPTLSYAGI EQSQIVVEAV VENPKIKAAV LAETESHIND
     DCILASNTST IPITELAKSL KRPENFCGMH FFNPVHRMPL VEIIRGEKTS DKTISTVVAY
     ASKMGKTPIV VNDCPGFFVN RVLFPYLAGF GMLLRDGGDF RQIDKIMEKE FGWPMGPAYL
     IDVVGIDTAH HAQAVMAQGF PERMTRDYHD AIDVLFENQR YGQKNDVGFY KYTQDKKGKP
     KKEQDETVDQ LLAGISHPKQ IFSGEDIIAR TMIPMINEVV RCLEEGVIAS PAEADMALVY
     GLGFPPFHGG VFRYLDTMGT AAYVKLAERY AHLGAMYHVP AGLKAKSESN ESYYPAAAKI
     AVNPGEKA
//

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