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
