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Protein
Submitted name:

3-hydroxyacyl-CoA dehydrogenase

Gene

fadB

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei175 – 1751Coenzyme ACombined sources
Binding sitei308 – 3081Coenzyme ACombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi629 – 6335ADPCombined sources

GO - Molecular functioni

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

GO - Biological processi

  1. fatty acid metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseSAAS annotation

Keywords - Biological processi

Fatty acid metabolismSAAS annotation, Lipid metabolism

Keywords - Ligandi

NADSAAS annotation, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciMTBRV:RV0860-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
3-hydroxyacyl-CoA dehydrogenaseImported
Submitted name:
FadB proteinImported
Submitted name:
Fatty oxidation protein FadBImported
Gene namesi
Name:fadBImported
Ordered Locus Names:Rv0860Imported, RVBD_0860Imported
ORF Names:LH57_04690Imported, P425_00900Imported
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)Imported
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001584 Componenti: Chromosome UP000003123 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cell wall Source: MTBBASE
  2. cytosol Source: MTBBASE
  3. plasma membrane Source: MTBBASE
Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv0860.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B3HX-ray2.30A/B1-720[»]
4B3IX-ray2.63A/B1-720[»]
4B3JX-ray2.50A/B1-720[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 716Coenzyme A bindingCombined sources

Phylogenomic databases

HOGENOMiHOG000261345.
KOiK01782.
OMAiMMMLNEA.
OrthoDBiEOG6M9F0M.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
3.90.226.10. 2 hits.
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. 1 hit.
PF02737. 3HCDH_N. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF52096. SSF52096. 1 hit.

Sequencei

Sequence statusi: Complete.

O53872-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDNTIQWDK DADGIVTLTM DDPSGSTNVM NEAYIESMGK AVDRLVAEKD
60 70 80 90 100
SITGVVVASA KKTFFAGGDV KTMIQARPED AGDVFNTVET IKRQLRTLET
110 120 130 140 150
LGKPVVAAIN GAALGGGLEI ALACHHRIAA DVKGSQLGLP EVTLGLLPGG
160 170 180 190 200
GGVTRTVRMF GIQNAFVSVL AQGTRFKPAK AKEIGLVDEL VATVEELVPA
210 220 230 240 250
AKAWIKEELK ANPDGAGVQP WDKKGYKMPG GTPSSPGLAA ILPSFPSNLR
260 270 280 290 300
KQLKGAPMPA PRAILAAAVE GAQVDFDTAS RIESRYFASL VTGQVAKNMM
310 320 330 340 350
QAFFFDLQAI NAGGSRPEGI GKTPIKRIGV LGAGMMGAGI AYVSAKAGYE
360 370 380 390 400
VVLKDVSLEA AAKGKGYSEK LEAKALERGR TTQERSDALL ARITPTADAA
410 420 430 440 450
DFKGVDFVIE AVFENQELKH KVFGEIEDIV EPNAILGSNT STLPITGLAT
460 470 480 490 500
GVKRQEDFIG IHFFSPVDKM PLVEIIKGEK TSDEALARVF DYTLAIGKTP
510 520 530 540 550
IVVNDSRGFF TSRVIGTFVN EALAMLGEGV EPASIEQAGS QAGYPAPPLQ
560 570 580 590 600
LSDELNLELM HKIAVATRKG VEDAGGTYQP HPAEAVVEKM IELGRSGRLK
610 620 630 640 650
GAGFYEYADG KRSGLWPGLR ETFKSGSSQP PLQDMIDRML FAEALETQKC
660 670 680 690 700
LDEGVLTSTA DANIGSIMGI GFPPWTGGSA QFIVGYSGPA GTGKAAFVAR
710 720
ARELAAAYGD RFLPPESLLS
Length:720
Mass (Da):76,104
Last modified:June 1, 1998 - v1
Checksum:i52CB1865400F3BE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003248 Genomic DNA. Translation: AFN48740.1.
CP009480 Genomic DNA. Translation: AIR13593.1.
AL123456 Genomic DNA. Translation: CCP43608.1.
JLDD01000008 Genomic DNA. Translation: KBJ39059.1.
RefSeqiNP_215375.1. NC_000962.3.
YP_006514211.1. NC_018143.2.

Genome annotation databases

EnsemblBacteriaiAFN48740; AFN48740; RVBD_0860.
CCP43608; CCP43608; Rv0860.
KBJ39059; KBJ39059; P425_00900.
GeneIDi885799.
KEGGimtu:Rv0860.
mtv:RVBD_0860.
PATRICi18150437. VBIMycTub87468_0961.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP003248 Genomic DNA. Translation: AFN48740.1.
CP009480 Genomic DNA. Translation: AIR13593.1.
AL123456 Genomic DNA. Translation: CCP43608.1.
JLDD01000008 Genomic DNA. Translation: KBJ39059.1.
RefSeqiNP_215375.1. NC_000962.3.
YP_006514211.1. NC_018143.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B3HX-ray2.30A/B1-720[»]
4B3IX-ray2.63A/B1-720[»]
4B3JX-ray2.50A/B1-720[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv0860.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAFN48740; AFN48740; RVBD_0860.
CCP43608; CCP43608; Rv0860.
KBJ39059; KBJ39059; P425_00900.
GeneIDi885799.
KEGGimtu:Rv0860.
mtv:RVBD_0860.
PATRICi18150437. VBIMycTub87468_0961.

Phylogenomic databases

HOGENOMiHOG000261345.
KOiK01782.
OMAiMMMLNEA.
OrthoDBiEOG6M9F0M.

Enzyme and pathway databases

BioCyciMTBRV:RV0860-MONOMER.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
3.90.226.10. 2 hits.
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. 1 hit.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37RvImported and H37RvImported.
  2. "Re-annotation of the genome sequence of Mycobacterium tuberculosis H37Rv."
    Camus J.C., Pryor M.J., Medigue C., Cole S.T.
    Microbiology 148:2967-2973(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: H37RvImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: H37RvImported.
  4. Lew J.M.
    Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: H37RvImported.
  5. "Structure of mycobacterial beta-oxidation trifunctional enzyme reveals its altered assembly and putative substrate channeling pathway."
    Venkatesan R., Wierenga R.K.
    ACS Chem. Biol. 8:1063-1073(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ADP AND COENZYME A.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37RvImported.
  7. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: H37RvImported.
  8. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: H37RvImported.
  9. "Phylogenetic analysis of Mycobacterial species using whole genome sequences."
    Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J., Monaco A., King S., Sohrabi A.
    Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: H37RvImported.

Entry informationi

Entry nameiO53872_MYCTU
AccessioniPrimary (citable) accession number: O53872
Secondary accession number(s): F2GIZ3, I6Y8Y4
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 1998
Last sequence update: June 1, 1998
Last modified: April 29, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.