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C3LSI3

- FADB_VIBCM

UniProt

C3LSI3 - FADB_VIBCM

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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Vibrio cholerae serotype O1 (strain M66-2)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.UniRule annotation

Catalytic activityi

(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH.UniRule annotation
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O.UniRule annotation
(S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA.UniRule annotation
(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei119 – 1191Important for catalytic activityUniRule annotation
Sitei139 – 1391Important for catalytic activityUniRule annotation
Binding sitei296 – 2961SubstrateUniRule annotation
Binding sitei325 – 3251NAD; via amide nitrogenUniRule annotation
Binding sitei344 – 3441NADUniRule annotation
Binding sitei408 – 4081NADUniRule annotation
Active sitei451 – 4511For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
Binding sitei454 – 4541NADUniRule annotation
Binding sitei501 – 5011SubstrateUniRule annotation
Binding sitei661 – 6611SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi401 – 4033NADUniRule annotation
Nucleotide bindingi428 – 4303NADUniRule annotation

GO - Molecular functioni

  1. 3-hydroxyacyl-CoA dehydrogenase activity Source: UniProtKB-HAMAP
  2. 3-hydroxybutyryl-CoA epimerase activity Source: UniProtKB-HAMAP
  3. coenzyme binding Source: InterPro
  4. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB-HAMAP
  5. enoyl-CoA hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fatty acid beta-oxidation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid degradation, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciVCHO579112:GJAW-2767-MONOMER.
UniPathwayiUPA00659.

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid oxidation complex subunit alphaUniRule annotation
Including the following 2 domains:
Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimeraseUniRule annotation (EC:4.2.1.17UniRule annotation, EC:5.1.2.3UniRule annotation, EC:5.3.3.8UniRule annotation)
3-hydroxyacyl-CoA dehydrogenaseUniRule annotation (EC:1.1.1.35UniRule annotation)
Gene namesi
Name:fadBUniRule annotation
Ordered Locus Names:VCM66_2678
OrganismiVibrio cholerae serotype O1 (strain M66-2)
Taxonomic identifieri579112 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000001217: Chromosome I

Subcellular locationi

GO - Cellular componenti

  1. fatty acid beta-oxidation multienzyme complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 723723Fatty acid oxidation complex subunit alphaPRO_1000186057Add
BLAST

Interactioni

Subunit structurei

Heterotetramer of two alpha chains (FadB) and two beta chains (FadA).UniRule annotation

Protein-protein interaction databases

STRINGi579112.VCM66_2678.

Structurei

3D structure databases

ProteinModelPortaliC3LSI3.
SMRiC3LSI3. Positions 1-716.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 189189Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
BLAST
Regioni311 – 7234133-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.UniRule annotation
In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1250.
HOGENOMiHOG000261344.
KOiK01825.
OMAiAKGMVMQ.
OrthoDBiEOG6M9F0M.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 2 hits.
HAMAPiMF_01621. FadB.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
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.
IPR012799. FadB.
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.
TIGRFAMsiTIGR02437. FadB. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C3LSI3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIYQAKTLQV KQLANGIAEL SFCAPASVNK LDLHTLESLD KALDALAADS
60 70 80 90 100
SVKGLLLSSD KEAFIVGADI TEFLGLFAKP EAELDEWLQF ANRIFNKLED
110 120 130 140 150
LPFPTLSALK GHTLGGGCEC VLATDFRIGD ATTSIGLPET KLGIMPGFGG
160 170 180 190 200
TVRLPRLIGA DSAMEIITQG KACRAEEALK VGLLDAIVDS DKLIDSAITT
210 220 230 240 250
LTQAIEEKLD WQKRRQQKTS ALTLSKLEAM MSFTMAKGMV AQVAGKHYPA
260 270 280 290 300
PMTSVVTIEE AARLPRDAAL DIERKHFIKL AKSTEAQALV GIFLNDQYIK
310 320 330 340 350
GLAKQSAKAA SQDTQHAAVL GAGIMGGGIA YQSALKGVPV LMKDIAPHSL
360 370 380 390 400
ELGMTEAAKL LNKQLERGKI DGFKMAGILA SITPSLHYAG IDQADVIVEA
410 420 430 440 450
VVENPKVKAA VLSEVEGLVD TETILTSNTS TIPINLLAKS LKRPQNFCGM
460 470 480 490 500
HFFNPVHRMP LVEIIRGEHT SEDTINRVVA YAAKMGKSPI VVNDCPGFFV
510 520 530 540 550
NRVLFPYFAG FSLLMRDGAN FTEIDKVMER QFGWPMGPAY LLDVVGIDTA
560 570 580 590 600
HHAQAVMAEG FPTRMAKSGR EAIDALYEAK KFGQKNGSGF YQYTVDKKGK
610 620 630 640 650
PKKAFSDDVL AILAPVCGAP QSFDPQTLIE RTMIPMINEV VLCLEEGIIA
660 670 680 690 700
SAQEADMALV YGLGFPPFRG GVFRYLDTIG IANYVAMAEK YADLGALYQV
710 720
PQLLKNMAQQ GTSFYSAQQV SAL
Length:723
Mass (Da):78,108
Last modified:June 16, 2009 - v1
Checksum:i147F5ABD0B0797F8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001233 Genomic DNA. Translation: ACP06970.1.
RefSeqiYP_002811421.1. NC_012578.1.

Genome annotation databases

EnsemblBacteriaiACP06970; ACP06970; VCM66_2678.
GeneIDi7773931.
KEGGivcm:VCM66_2678.
PATRICi20069086. VBIVibCho108967_2554.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001233 Genomic DNA. Translation: ACP06970.1 .
RefSeqi YP_002811421.1. NC_012578.1.

3D structure databases

ProteinModelPortali C3LSI3.
SMRi C3LSI3. Positions 1-716.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 579112.VCM66_2678.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACP06970 ; ACP06970 ; VCM66_2678 .
GeneIDi 7773931.
KEGGi vcm:VCM66_2678.
PATRICi 20069086. VBIVibCho108967_2554.

Phylogenomic databases

eggNOGi COG1250.
HOGENOMi HOG000261344.
KOi K01825.
OMAi AKGMVMQ.
OrthoDBi EOG6M9F0M.

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci VCHO579112:GJAW-2767-MONOMER.

Family and domain databases

Gene3Di 1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 2 hits.
HAMAPi MF_01621. FadB.
InterProi IPR006180. 3-OHacyl-CoA_DH_CS.
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.
IPR012799. FadB.
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.
TIGRFAMsi TIGR02437. FadB. 1 hit.
PROSITEi PS00067. 3HCDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "A recalibrated molecular clock and independent origins for the cholera pandemic clones."
    Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
    PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: M66-2.

Entry informationi

Entry nameiFADB_VIBCM
AccessioniPrimary (citable) accession number: C3LSI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 16, 2009
Last modified: October 1, 2014
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3