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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Shewanella sp. (strain MR-4)
Status
Reviewed-Annotation score: -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
A (3Z)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA.UniRule annotation
A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA.UniRule annotation

Pathwayi: fatty acid beta-oxidation

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei119Important for catalytic activityUniRule annotation1
Sitei139Important for catalytic activityUniRule annotation1
Binding sitei296SubstrateUniRule annotation1
Binding sitei324NAD; via amide nitrogenUniRule annotation1
Binding sitei343NADUniRule annotation1
Binding sitei407NADUniRule annotation1
Binding sitei429NADUniRule annotation1
Active sitei450For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation1
Binding sitei453NADUniRule annotation1
Binding sitei500SubstrateUniRule annotation1
Binding sitei660SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi400 – 402NADUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Lyase, Multifunctional enzyme, Oxidoreductase
Biological processFatty acid metabolism, Lipid degradation, Lipid metabolism
LigandNAD

Enzyme and pathway databases

BioCyciSSP60480:G1G76-17-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:Shewmr4_0018
OrganismiShewanella sp. (strain MR-4)
Taxonomic identifieri60480 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000695791 – 716Fatty acid oxidation complex subunit alphaAdd BLAST716

Proteomic databases

PRIDEiQ0HPB7

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ0HPB7
SMRiQ0HPB7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 189Enoyl-CoA hydratase/isomeraseUniRule annotationAdd BLAST189
Regioni311 – 7163-hydroxyacyl-CoA dehydrogenaseUniRule annotationAdd BLAST406

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

HOGENOMiHOG000261344
KOiK01825
OMAiDYKAKRQ

Family and domain databases

HAMAPiMF_01621 FadB, 1 hit
InterProiView protein in InterPro
IPR006180 3-OHacyl-CoA_DH_CS
IPR006176 3-OHacyl-CoA_DH_NAD-bd
IPR006108 3HC_DH_C
IPR008927 6-PGluconate_DH-like_C_sf
IPR029045 ClpP/crotonase-like_dom_sf
IPR001753 Enoyl-CoA_hydra/iso
IPR012799 FadB
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF00725 3HCDH, 1 hit
PF02737 3HCDH_N, 1 hit
PF00378 ECH_1, 1 hit
SUPFAMiSSF48179 SSF48179, 2 hits
SSF51735 SSF51735, 1 hit
SSF52096 SSF52096, 1 hit
TIGRFAMsiTIGR02437 FadB, 1 hit
PROSITEiView protein in PROSITE
PS00067 3HCDH, 1 hit

Sequencei

Sequence statusi: Complete.

Q0HPB7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIYQSPTIQV ELLEDNIAKL CFNAPGSVNK FDRETLASLD AALDSIKQQS
60 70 80 90 100
NIQALVLTSG KDTFIVGADI TEFLGLFAQD DAVLLSWVEQ ANAVFNKLED
110 120 130 140 150
LPFPTASAIK GFALGGGCEA ILATDFRIAD TTAKIGLPET KLGIIPGFGG
160 170 180 190 200
TVRLPRVIGA DNALEWITTG KDQRPEDALK VGAVDAVVAP EALEAAAIQM
210 220 230 240 250
LKDAVAEKLD WQARRQRKMS PLTLPKLEAM MSFTTAKGMV FAVAGKHYPA
260 270 280 290 300
PMAAVSVVEQ AATKGRSDAL QIEHQAFIKL AKTDVAKALI GIFLNDQLVK
310 320 330 340 350
GKAKKAGKLA KDVKSAAVLG AGIMGGGIAY QSASKGTPIV MKDIAQPALD
360 370 380 390 400
LGLGEAAKLL SAQVARGRST PEKMAKVLNN ITPALDYAPV KHADVVVEAV
410 420 430 440 450
VEHPKVKAQV LAEVEQYVSE DAIIASNTST ISINLLAKSM KKPERFCGMH
460 470 480 490 500
FFNPVHKMPL VEVIRGEHSS EETIASVVAY ASKMGKTPIV VNDCPGFFVN
510 520 530 540 550
RVLFPYFAGF NGLLAEGGDF AAIDKVMEKQ FGWPMGPAYL LDVVGLDTGH
560 570 580 590 600
HAQAVMAEGF PDRMGKSGND AIDVMFENKR LGQKNGKGFY AYSVDSRGKP
610 620 630 640 650
KKDVDPTSYE LLKAAFGEQK AFDADEIIAR TMIPMIIETV RCLEEGIVAS
660 670 680 690 700
PAEADMGLVY GLGFPPFRGG VFRYLDTMGV ANFVALADKY AHLGGLYQVT
710
DAMRTLAANN GSYYQA
Length:716
Mass (Da):76,646
Last modified:October 3, 2006 - v1
Checksum:iDBF1266FA2C38F82
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000446 Genomic DNA Translation: ABI37100.1
RefSeqiWP_011620854.1, NC_008321.1

Genome annotation databases

EnsemblBacteriaiABI37100; ABI37100; Shewmr4_0018
KEGGishe:Shewmr4_0018

Entry informationi

Entry nameiFADB_SHESM
AccessioniPrimary (citable) accession number: Q0HPB7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 3, 2006
Last modified: May 23, 2018
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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

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