(data stored in ACNUC7421 zone)

SWISSPROT: FADB_AERHH

ID   FADB_AERHH              Reviewed;         715 AA.
AC   A0KEL1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   11-DEC-2019, entry version 100.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000255|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:0000255|HAMAP-Rule:MF_01621};
DE              EC=4.2.1.17 {ECO:0000255|HAMAP-Rule:MF_01621};
DE              EC=5.1.2.3 {ECO:0000255|HAMAP-Rule:MF_01621};
DE              EC=5.3.3.8 {ECO:0000255|HAMAP-Rule:MF_01621};
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01621};
DE              EC=1.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01621};
GN   Name=fadB {ECO:0000255|HAMAP-Rule:MF_01621}; OrderedLocusNames=AHA_0139;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM
OS   1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- FUNCTION: Involved in the aerobic and anaerobic degradation of long-
CC       chain fatty acids via beta-oxidation cycle. Catalyzes the formation of
CC       3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use
CC       D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
CC       {ECO:0000255|HAMAP-Rule:MF_01621}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01621};
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:0000255|HAMAP-
CC         Rule:MF_01621};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC         ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01621};
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:0000255|HAMAP-Rule:MF_01621};
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:0000255|HAMAP-Rule:MF_01621};
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:0000255|HAMAP-Rule:MF_01621};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000255|HAMAP-Rule:MF_01621}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains
CC       (FadA). {ECO:0000255|HAMAP-Rule:MF_01621}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000255|HAMAP-Rule:MF_01621}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01621}.
DR   EMBL; CP000462; ABK38031.1; -; Genomic_DNA.
DR   RefSeq; WP_011704165.1; NC_008570.1.
DR   RefSeq; YP_854676.1; NC_008570.1.
DR   SMR; A0KEL1; -.
DR   STRING; 380703.AHA_0139; -.
DR   PRIDE; A0KEL1; -.
DR   EnsemblBacteria; ABK38031; ABK38031; AHA_0139.
DR   GeneID; 4490320; -.
DR   KEGG; aha:AHA_0139; -.
DR   PATRIC; fig|380703.7.peg.132; -.
DR   eggNOG; ENOG4105DYT; Bacteria.
DR   eggNOG; COG1024; LUCA.
DR   eggNOG; COG1250; LUCA.
DR   HOGENOM; HOG000261344; -.
DR   KO; K01825; -.
DR   OMA; TGAGWPF; -.
DR   BioCyc; AHYD380703:G1G7B-139-MONOMER; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000000756; 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; 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.
PE   3: Inferred from homology;
DR   PRODOM; A0KEL1.
DR   SWISS-2DPAGE; A0KEL1.
KW   Fatty acid metabolism; Isomerase; Lipid degradation; Lipid metabolism;
KW   Lyase; Multifunctional enzyme; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..715
FT                   /note="Fatty acid oxidation complex subunit alpha"
FT                   /id="PRO_1000069557"
FT   NP_BIND         401..403
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   REGION          1..189
FT                   /note="Enoyl-CoA hydratase/isomerase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   REGION          311..715
FT                   /note="3-hydroxyacyl-CoA dehydrogenase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   ACT_SITE        451
FT                   /note="For 3-hydroxyacyl-CoA dehydrogenase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         296
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         325
FT                   /note="NAD; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         344
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         408
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         430
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         454
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         501
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         661
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   SITE            119
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   SITE            139
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
SQ   SEQUENCE   715 AA;  76523 MW;  41DF8B6A84E7751A CRC64;
     MIYQGETLTV SYLEDGIAEL RFDAPGSVNK LDRATLLSLS EAIAALQQER ELKGLILTSG
     KDAFIVGADI TEFLELFDLP QADLLGWLKK ANDIFSAIED LPVPTLSAIK GHALGGGCET
     ILSTDFRLAD TSAKIGLPET KLGIMPGFGG TVRLPRVIGA DNALEWITTG KDYRADDALK
     VGAIDAVVAP DALQSAAVQM IKDAVKGKLD WQGRRAAKKA PLRLSKLEAM MSFTTAAGMV
     AAVAGKHYPA PMTAVKTVEA AAGMSRDEAL AVEAQGFIKL AKTDVAKALV GIFLNDQHIK
     ALAKKAAKQA AKATSHAAVL GAGIMGGGIA YQSASKGIPA VMKDINEKAL ALGMGEATKL
     LNGQLEKGRI DGIKMGQVLS AITPTLSYDN VKHVDVVVEA VVENPKVKAA VLGEVEGIIG
     EDAVLASNTS TIPISLLAKE LKRPQNFCGM HFFNPVHRMP LVEIIRGEQT SDETINRVVA
     YAAAMGKSPV VVNDCPGFFV NRVLFPYFFG FNKLVADGAD FAAVDKVMEK EFGWPMGPAY
     LLDVVGIDTG HHAGDVMAQG FPARMSKEGR TAIDVMYEVN RFGQKNGKGF YAYEQDKKGK
     PKKVADAASY ELLAPIAKPK QDFDKDAIIA RMMIPMINEV VLCLEEGIVA TPAEADIALV
     YGLGFPPFRG GVFRYLDTIG LDRYVAMADQ YADLGPLYRV SDKLREMAAQ GKTFY
//

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