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Protein

Probable 3-hydroxyacyl-CoA dehydrogenase

Gene

fadN

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in the degradation of long-chain fatty acids.

Catalytic activityi

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.

Pathway: fatty acid beta-oxidation

This protein is involved in the pathway fatty acid beta-oxidation, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid beta-oxidation and in Lipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid degradation, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciBSUB:BSU32840-MONOMER.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 3-hydroxyacyl-CoA dehydrogenase (EC:1.1.1.35)
Gene namesi
Name:fadN
Synonyms:yusL
Ordered Locus Names:BSU32840
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU32840. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 789789Probable 3-hydroxyacyl-CoA dehydrogenasePRO_0000360673Add
BLAST

Proteomic databases

PaxDbiO32178.

Expressioni

Inductioni

Repressed by FadR in the absence of LCFAs (fatty acids of 14-20 carbon atoms). When LCFAs are present in the medium, they are converted to long-chain acyl-CoAs, which antagonize FadR as to its binding to fadR boxes on target DNA and thus derepress transcription.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100017816.

Structurei

3D structure databases

ProteinModelPortaliO32178.
SMRiO32178. Positions 2-439, 483-787.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000264370.
InParanoidiO32178.
OMAiMRWGFGW.
OrthoDBiEOG6B8XF5.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.

Sequencei

Sequence statusi: Complete.

O32178-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHKHIRKAAV LGSGVMGSGI AAHLANIGIP VLLLDIVPND LTKEEEKKGL
60 70 80 90 100
TKDSSEVRSR LSRQAMKKLL KQKPAPLTSA KNTSYITPGN LEDDAEKLKE
110 120 130 140 150
ADWIIEVVVE NLEVKKKIFA LVDEHRKTGS IVSSNTSGIS VQEMAEGRSD
160 170 180 190 200
DFKAHFLGTH FFNPARYLKL LEIIPIKETD PDILKFMTAF GENVLGKGVV
210 220 230 240 250
TAKDTPNFIA NRIGTYGLLV TVQEMLKGGY QVGEVDSITG PLIGRPKSAT
260 270 280 290 300
FRTLDVVGLD TFAHVARNVY DKADGDEKEV FRIPSFMNDM LEKGWIGSKA
310 320 330 340 350
GQGFYKKEGK TIYELDPVTL TYGERTKMKS PALEAAKQAK GTKAKMKALI
360 370 380 390 400
YSDDRAGRLL WNITSQTLLY SAELLGEIAD DIHAIDQAMK WGFGWELGPF
410 420 430 440 450
EMWDAIGLKQ SAEKLEQLGA DMPGWIKEML DKGNETFYIK ENGTVFYYDR
460 470 480 490 500
GEYRAVKENK KRIHLQALKE TKGVIAKNSG ASLIDLGDDV ALLEFHSKSN
510 520 530 540 550
AIGLDIIQMI HKGLEETERN YKGLVIGNQG KNFCVGANLA MILMEVQDDN
560 570 580 590 600
FLEVDFVIRR FQETMMKIKY SAKPVVAAPF GMTLGGGTEA CLPAARIQAA
610 620 630 640 650
SEAYMGLVES GVGLIPGGGG NKELYINHLR RGHDPMNAAM KTFETIAMAK
660 670 680 690 700
VSASAQEARE MNILKETDQI SVNQDHLLYD AKQLAASLYD TGWRPPVKEK
710 720 730 740 750
VKVPGETGYA ALLLGAEQMK LSGYISEHDF KIAKKLAYVI AGGKVPFGTE
760 770 780
VDEEYLLEIE REAFLSLSGE AKSQARMQHM LVKGKPLRN
Length:789
Mass (Da):87,085
Last modified:January 20, 2009 - v2
Checksum:i9379318D7E70F40C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15273.2.
PIRiE70021.
RefSeqiWP_003243831.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15273; CAB15273; BSU32840.
PATRICi18978548. VBIBacSub10457_3437.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15273.2.
PIRiE70021.
RefSeqiWP_003243831.1. NZ_JNCM01000033.1.

3D structure databases

ProteinModelPortaliO32178.
SMRiO32178. Positions 2-439, 483-787.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100017816.

Proteomic databases

PaxDbiO32178.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15273; CAB15273; BSU32840.
PATRICi18978548. VBIBacSub10457_3437.

Organism-specific databases

GenoListiBSU32840. [Micado]

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000264370.
InParanoidiO32178.
OMAiMRWGFGW.
OrthoDBiEOG6B8XF5.

Enzyme and pathway databases

UniPathwayiUPA00659.
BioCyciBSUB:BSU32840-MONOMER.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "Organization and function of the YsiA regulon of Bacillus subtilis involved in fatty acid degradation."
    Matsuoka H., Hirooka K., Fujita Y.
    J. Biol. Chem. 282:5180-5194(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, GENE NAME, IDENTIFICATION OF INITIATION SITE.
    Strain: 168.

Entry informationi

Entry nameiFADN_BACSU
AccessioniPrimary (citable) accession number: O32178
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 20, 2009
Last modified: June 24, 2015
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.