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Q4FQC6

- FADB_PSYA2

UniProt

Q4FQC6 - FADB_PSYA2

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Protein

Fatty acid oxidation complex subunit alpha

Gene

fadB

Organism
Psychrobacter arcticus (strain DSM 17307 / 273-4)
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
Sitei120 – 1201Important for catalytic activityUniRule annotation
Sitei140 – 1401Important for catalytic activityUniRule annotation
Binding sitei298 – 2981SubstrateUniRule annotation
Binding sitei326 – 3261NAD; via amide nitrogenUniRule annotation
Binding sitei345 – 3451NADUniRule annotation
Binding sitei409 – 4091NADUniRule annotation
Active sitei452 – 4521For 3-hydroxyacyl-CoA dehydrogenase activityUniRule annotation
Binding sitei455 – 4551NADUniRule annotation
Binding sitei502 – 5021SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi402 – 4043NADUniRule annotation
Nucleotide bindingi429 – 4313NADUniRule 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

BioCyciPARC259536:GI3A-1979-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:Psyc_1934
OrganismiPsychrobacter arcticus (strain DSM 17307 / 273-4)
Taxonomic identifieri259536 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter
ProteomesiUP000000546: Chromosome

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 – 719719Fatty acid oxidation complex subunit alphaPRO_0000109283Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi259536.Psyc_1934.

Structurei

3D structure databases

ProteinModelPortaliQ4FQC6.
SMRiQ4FQC6. Positions 1-717.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 190190Enoyl-CoA hydratase/isomeraseUniRule annotationAdd
BLAST
Regioni313 – 7194073-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. 1 hit.
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.

Q4FQC6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVYQGNRITV TMLEDGIANM QYNAENESVN KFDTETNKQF AEVVNALEKA
60 70 80 90 100
DDVKGLIVTS SKGVFIAGAD ITEFVASFKQ SEEEIKDWVI NINDAFNRFE
110 120 130 140 150
DLPFPKVAAI NGAALGGGCE MTLVCEYRVM SDKAIIGLPE TQLGIFPGFG
160 170 180 190 200
GTVRSTRVIG IDNALELIAT GAPKKALDAL KLGLVDATVA ADDLQDAAID
210 220 230 240 250
LVKKCISGEL DWKAKREEKL VAVKLNQLEQ AMAFNSAKGM IFAKANPKQY
260 270 280 290 300
PAPALAIAAI EKHVNLPRDK AIEVEAAGFA KAAKTPQAES LVGLFLSDQL
310 320 330 340 350
VKKLAKQHSK KAHEINEAAV LGAGIMGGGI AYQAASKGLP IIMKDIKSEQ
360 370 380 390 400
LDLGMGEASK LLGKMVDRGK MTPAKMGETL SRIRPTLNYG DFAETDIVIE
410 420 430 440 450
AVVENPNVKR AVLKEVEGLV KDDCILASNT STISITFLAE ALERPENFVG
460 470 480 490 500
MHFFNPVHRM PLVEVIRGEK SSEEAIATTV ALASKMGKVP VVVNDCPGFL
510 520 530 540 550
VNRVLFPYFG AFDLLLKQGA DFAHVDKVME KFGWPMGPAY LIDVVGLDTG
560 570 580 590 600
VHGAEVMAEG FPDRMKPDYK GAIELLYENK RLGQKNGVGF YKYEMDKRGK
610 620 630 640 650
PKKVADEATY ELLKTTTDSE KQTFDDQAII DRTMLAFCNE TVRCLEDNIV
660 670 680 690 700
STPSEADMAM IMGVGFPPFR GGPCRYIDQM GLDNYLALCE KYAHLGKAYE
710
APQKIRDMAA AGETFYATA
Length:719
Mass (Da):78,225
Last modified:August 30, 2005 - v1
Checksum:i67B55A992065C896
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000082 Genomic DNA. Translation: AAZ19782.1.
RefSeqiYP_265216.1. NC_007204.1.

Genome annotation databases

EnsemblBacteriaiAAZ19782; AAZ19782; Psyc_1934.
GeneIDi3515904.
KEGGipar:Psyc_1934.
PATRICi23058763. VBIPsyArc98534_2286.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000082 Genomic DNA. Translation: AAZ19782.1 .
RefSeqi YP_265216.1. NC_007204.1.

3D structure databases

ProteinModelPortali Q4FQC6.
SMRi Q4FQC6. Positions 1-717.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 259536.Psyc_1934.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ19782 ; AAZ19782 ; Psyc_1934 .
GeneIDi 3515904.
KEGGi par:Psyc_1934.
PATRICi 23058763. VBIPsyArc98534_2286.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00659 .
BioCyci PARC259536:GI3A-1979-MONOMER.

Family and domain databases

Gene3Di 1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
3.90.226.10. 1 hit.
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. "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
    Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
    Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 17307 / 273-4.

Entry informationi

Entry nameiFADB_PSYA2
AccessioniPrimary (citable) accession number: Q4FQC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: August 30, 2005
Last modified: October 1, 2014
This is version 73 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, Reference proteome

Documents

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

External Data

Dasty 3