ID FADB_KLEP7 Reviewed; 729 AA.
AC A6TGM4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 07-JUN-2017, entry version 73.
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};
GN OrderedLocusNames=KPN78578_42840; ORFNames=KPN_04340;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH
OS 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-Rule:MF_01621}.
CC -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC + NADH. {ECO:0000255|HAMAP-Rule:MF_01621}.
CC -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CC CoA + H(2)O. {ECO:0000255|HAMAP-Rule:MF_01621}.
CC -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
CC hydroxybutanoyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01621}.
CC -!- CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-
CC CoA. {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
CC chains (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-
CC hydroxyacyl-CoA dehydrogenase family. {ECO:0000255|HAMAP-
CC Rule:MF_01621}.
DR EMBL; CP000647; ABR79708.1; -; Genomic_DNA.
DR RefSeq; WP_004901902.1; NC_009648.1.
DR ProteinModelPortal; A6TGM4; -.
DR SMR; A6TGM4; -.
DR STRING; 272620.KPN_04340; -.
DR EnsemblBacteria; ABR79708; ABR79708; KPN_04340.
DR KEGG; kpn:KPN_04340; -.
DR eggNOG; ENOG4108EIM; Bacteria.
DR eggNOG; COG1024; LUCA.
DR eggNOG; COG1250; LUCA.
DR HOGENOM; HOG000261344; -.
DR KO; K01825; -.
DR OMA; IDLCMIL; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000000265; 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-EC.
DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.1040.10; -; 2.
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_C-like.
DR InterPro; IPR013328; 6PGD_dom_2.
DR InterPro; IPR029045; ClpP/crotonase-like_dom.
DR InterPro; IPR001753; Crotonase_core_superfam.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR012799; FadB.
DR InterPro; IPR016040; NAD(P)-bd_dom.
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;
KW Complete proteome; Fatty acid metabolism; Isomerase;
KW Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1 729 Fatty acid oxidation complex subunit
FT alpha.
FT /FTId=PRO_1000069564.
FT NP_BIND 400 402 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT REGION 1 189 Enoyl-CoA hydratase/isomerase.
FT {ECO:0000255|HAMAP-Rule:MF_01621}.
FT REGION 311 729 3-hydroxyacyl-CoA dehydrogenase.
FT {ECO:0000255|HAMAP-Rule:MF_01621}.
FT ACT_SITE 450 450 For 3-hydroxyacyl-CoA dehydrogenase
FT activity. {ECO:0000255|HAMAP-
FT Rule:MF_01621}.
FT BINDING 296 296 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_01621}.
FT BINDING 324 324 NAD; via amide nitrogen.
FT {ECO:0000255|HAMAP-Rule:MF_01621}.
FT BINDING 343 343 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT BINDING 407 407 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT BINDING 429 429 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT BINDING 453 453 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT BINDING 500 500 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_01621}.
FT BINDING 660 660 Substrate. {ECO:0000255|HAMAP-
FT Rule:MF_01621}.
FT SITE 119 119 Important for catalytic activity.
FT {ECO:0000255|HAMAP-Rule:MF_01621}.
FT SITE 139 139 Important for catalytic activity.
FT {ECO:0000255|HAMAP-Rule:MF_01621}.
SQ SEQUENCE 729 AA; 79287 MW; 343B3315323919BB CRC64;
MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG HALDVLEKQS DLKGLLLRSE
KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTISAVN GYALGGGCEC
VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRLPRLLGA DSALEIIAAG KDVGADQALK
IGLVDGVVAA EKLRDGALAI LRQAMNGDLD WKAKRQPKLE PLKLSKIEAA MSFTIAKGMV
AQTAGKHYPA PITAVKTIEA AARLGREEAL VLENKSFVPL AHTNEARALV GIFLNDQYVK
AKAKKLTKDV ETPKHAAVLG AGIMGGGIAY QSAWKGVPVV MKDISDKSLT LGMTEAAKLL
NKQLERGKID GLKLAGVIST IQPTLEYSGF DRVDVVVEAV VENPKVKKAV LAETESKVRP
DTVLASNTST IPISELASVL QRPENFCGMH FFNPVHRMPL VEVIRGEKTS DNTIAKVVAW
ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKVDKVMEKQ FGWPMGPAYL
LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKDDSKGKP
KKEEDAAVDS LLADVSQPKR DFSDEEIIAR MMIPMVNEVV RCLEEGIIAS PAEADMALVY
GLGFPPFHGG AFRWLDTIGS AKYLDMAQQY QHLGPLYEVP AGLRDKARHN EAYYPQVEPA
RPVGALKTA
//
