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O32178

- FADN_BACSU

UniProt

O32178 - FADN_BACSU

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Protein

Probable 3-hydroxyacyl-CoA dehydrogenase

Gene

fadN

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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.

Pathwayi

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-EC
  2. coenzyme binding Source: InterPro

GO - Biological processi

  1. fatty acid beta-oxidation Source: UniProtKB-UniPathway
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: 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.BSU32840.

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000264370.
InParanoidiO32178.
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.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
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.

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 .
PIRi E70021.

3D structure databases

ProteinModelPortali O32178.
SMRi O32178. Positions 2-439, 483-787.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU32840.

Proteomic databases

PaxDbi O32178.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15273 ; CAB15273 ; BSU32840 .
PATRICi 18978548. VBIBacSub10457_3437.

Organism-specific databases

GenoListi BSU32840. [Micado ]

Phylogenomic databases

eggNOGi COG1250.
HOGENOMi HOG000264370.
InParanoidi O32178.
OrthoDBi EOG6B8XF5.

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci BSUB:BSU32840-MONOMER.

Family and domain databases

Gene3Di 1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
InterProi IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR013328. DH_multihelical.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view ]
SUPFAMi SSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 97 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