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FADJ_ECOLI
ID   FADJ_ECOLI              Reviewed;         714 AA.
AC   P77399; Q6KCX2;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 180.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha;
DE   Includes:
DE     RecName: Full=Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase;
DE              EC=4.2.1.17 {ECO:0000269|PubMed:12270828};
DE              EC=5.1.2.3;
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
DE              EC=1.1.1.35 {ECO:0000269|PubMed:12270828};
GN   Name=fadJ; Synonyms=yfcX; OrderedLocusNames=b2341, JW2338;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=12270828; DOI=10.1128/jb.184.20.5696-5705.2002;
RA   Snell K.D., Feng F., Zhong L., Martin D., Madison L.L.;
RT   "YfcX enables medium-chain-length poly(3-hydroxyalkanoate) formation from
RT   fatty acids in recombinant Escherichia coli fadB strains.";
RL   J. Bacteriol. 184:5696-5705(2002).
RN   [5]
RP   FUNCTION IN ANAEROBIC BETA-OXIDATION PATHWAY.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=12535077; DOI=10.1046/j.1365-2958.2003.03341.x;
RA   Campbell J.W., Morgan-Kiss R.M., Cronan J.E. Jr.;
RT   "A new Escherichia coli metabolic competency: growth on fatty acids by a
RT   novel anaerobic beta-oxidation pathway.";
RL   Mol. Microbiol. 47:793-805(2003).
CC   -!- FUNCTION: Catalyzes the formation of a hydroxyacyl-CoA by addition of
CC       water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-
CC       hydroxyacyl-CoA dehydrogenase activities. Strongly involved in the
CC       anaerobic degradation of long and medium-chain fatty acids in the
CC       presence of nitrate and weakly involved in the aerobic degradation of
CC       long-chain fatty acids. {ECO:0000269|PubMed:12270828,
CC       ECO:0000269|PubMed:12535077}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-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;
CC         Evidence={ECO:0000269|PubMed:12270828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-3-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;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-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:0000269|PubMed:12270828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA;
CC         Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316;
CC         EC=5.1.2.3;
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta chains
CC       (FadI). {ECO:0000250}.
CC   -!- INTERACTION:
CC       P77399; P77293: yfdH; NbExp=2; IntAct=EBI-545361, EBI-545379;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Unlike the aerobic pathway, the anaerobic pathway is not
CC       strongly repressed by FadR regulatory protein.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; U00096; AAC75401.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16195.1; -; Genomic_DNA.
DR   PIR; C65007; C65007.
DR   RefSeq; NP_416843.1; NC_000913.3.
DR   RefSeq; WP_000426176.1; NZ_LN832404.1.
DR   PDB; 6YSV; X-ray; 2.70 A; A/B=1-714.
DR   PDB; 6YSW; X-ray; 2.82 A; A/B=1-714.
DR   PDBsum; 6YSV; -.
DR   PDBsum; 6YSW; -.
DR   AlphaFoldDB; P77399; -.
DR   SASBDB; P77399; -.
DR   SMR; P77399; -.
DR   BioGRID; 4260533; 252.
DR   ComplexPortal; CPX-3966; fadJI fatty acid oxidation complex, anaerobic conditions.
DR   DIP; DIP-11990N; -.
DR   IntAct; P77399; 8.
DR   STRING; 511145.b2341; -.
DR   jPOST; P77399; -.
DR   PaxDb; P77399; -.
DR   PRIDE; P77399; -.
DR   EnsemblBacteria; AAC75401; AAC75401; b2341.
DR   EnsemblBacteria; BAA16195; BAA16195; BAA16195.
DR   GeneID; 949097; -.
DR   KEGG; ecj:JW2338; -.
DR   KEGG; eco:b2341; -.
DR   PATRIC; fig|1411691.4.peg.4391; -.
DR   EchoBASE; EB3879; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_16_1_6; -.
DR   InParanoid; P77399; -.
DR   OMA; PFRYMDT; -.
DR   PhylomeDB; P77399; -.
DR   BioCyc; EcoCyc:G7212-MON; -.
DR   BioCyc; MetaCyc:G7212-MON; -.
DR   UniPathway; UPA00659; -.
DR   PRO; PR:P77399; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IDA:ComplexPortal.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IDA:EcoCyc.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:EcoCyc.
DR   GO; GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IDA:ComplexPortal.
DR   HAMAP; MF_01617; FadJ; 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; IPR012802; FadJ.
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; TIGR02440; FadJ; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Fatty acid metabolism; Isomerase;
KW   Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme; NAD;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..714
FT                   /note="Fatty acid oxidation complex subunit alpha"
FT                   /id="PRO_0000109298"
FT   REGION          1..190
FT                   /note="Enoyl-CoA hydratase"
FT   REGION          306..714
FT                   /note="3-hydroxyacyl-CoA dehydrogenase"
FT   SITE            118
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            140
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   STRAND          6..11
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          15..21
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          24..28
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           33..35
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           36..46
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          54..58
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          61..66
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           72..75
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           80..98
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          101..108
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          110..113
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           115..122
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          123..129
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           139..143
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   TURN            148..150
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           151..154
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   TURN            155..158
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           161..170
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           176..181
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          184..189
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           191..193
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           194..203
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          204..206
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           214..218
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           222..240
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           245..259
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           262..278
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           280..297
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          300..303
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          311..314
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           317..329
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          335..338
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           342..360
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          361..364
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           367..373
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           374..376
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          377..383
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          390..394
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           400..413
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          419..422
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          425..427
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           429..432
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   TURN            433..435
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           439..441
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          442..446
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   TURN            451..453
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          456..461
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           467..479
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          483..486
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   TURN            491..494
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           495..511
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           516..526
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           532..539
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           541..545
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           548..555
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           557..559
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           565..570
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   TURN            571..573
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   TURN            577..580
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          581..584
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           601..604
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           615..635
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          638..641
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           642..652
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           657..659
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           662..669
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           671..684
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           687..689
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   HELIX           693..700
FT                   /evidence="ECO:0007829|PDB:6YSV"
FT   STRAND          705..708
FT                   /evidence="ECO:0007829|PDB:6YSV"
SQ   SEQUENCE   714 AA;  77072 MW;  F4E0A75680039A0D CRC64;
     MEMTSAFTLN VRLDNIAVIT IDVPGEKMNT LKAEFASQVR AIIKQLRENK ELRGVVFVSA
     KPDNFIAGAD INMIGNCKTA QEAEALARQG QQLMAEIHAL PIQVIAAIHG ACLGGGLELA
     LACHGRVCTD DPKTVLGLPE VQLGLLPGSG GTQRLPRLIG VSTALEMILT GKQLRAKQAL
     KLGLVDDVVP HSILLEAAVE LAKKERPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT
     QGNYPATERI LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRSIFF ASTDVKKDPG
     SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGIPVRIKDI NPQGINHALK YSWDQLEGKV
     RRRHLKASER DKQLALISGT TDYRGFAHRD LIIEAVFENL ELKQQMVAEV EQNCAAHTIF
     ASNTSSLPIG DIAAHATRPE QVIGLHFFSP VEKMPLVEII PHAGTSAQTI ATTVKLAKKQ
     GKTPIVVRDK AGFYVNRILA PYINEAIRML TQGERVEHID AALVKFGFPV GPIQLLDEVG
     IDTGTKIIPV LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA
     IYPLIGTQGQ GRISAPQVAE RCVMLMLNEA VRCVDEQVIR SVRDGDIGAV FGIGFPPFLG
     GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCERLVEMGA RGESFWKTTA TDLQ
 
 
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