SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P44432

- FABI_HAEIN

UniProt

P44432 - FABI_HAEIN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
Gene
fabI, envM, HI_1734
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism By similarity.

Catalytic activityi

An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.

Enzyme regulationi

Inhibited by 1,4-benzodiazepine and naphthyridinone derivatives.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei13 – 131NAD; via carbonyl oxygen By similarity
Binding sitei92 – 921NAD; via carbonyl oxygen By similarity
Binding sitei95 – 951Substrate; via amide nitrogen and carbonyl oxygen By similarity
Active sitei146 – 1461Proton acceptor By similarity
Active sitei156 – 1561Proton acceptor By similarity
Binding sitei163 – 1631NAD By similarity
Sitei201 – 2011Involved in acyl-ACP binding By similarity
Sitei204 – 2041Involved in acyl-ACP binding By similarity
Sitei205 – 2051Involved in acyl-ACP binding By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 202NAD By similarity
Nucleotide bindingi64 – 652NAD By similarity
Nucleotide bindingi192 – 1965NAD By similarity

GO - Molecular functioni

  1. enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: UniProtKB

GO - Biological processi

  1. fatty acid elongation Source: UniProtKB
  2. protein homotetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (EC:1.3.1.9)
Short name:
ENR
Alternative name(s):
NADH-dependent enoyl-ACP reductase
Gene namesi
Name:fabI
Synonyms:envM
Ordered Locus Names:HI_1734
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 262261Enoyl-[acyl-carrier-protein] reductase [NADH] FabI
PRO_0000054901Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi71421.HI1734.

Structurei

3D structure databases

ProteinModelPortaliP44432.
SMRiP44432. Positions 2-259.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0623.
KOiK00208.
OMAiGISGEIM.
OrthoDBiEOG6HF644.
PhylomeDBiP44432.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PIRSFiPIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSiPR00081. GDHRDH.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P44432-1 [UniParc]FASTAAdd to Basket

« Hide

MGFLTGKRIL VTGLASNRSI AYGIAKSMKE QGAELAFTYL NDKLQPRVEE    50
FAKEFGSDIV LPLDVATDES IQNCFAELSK RWDKFDGFIH AIAFAPGDQL 100
DGDYVNAATR EGYRIAHDIS AYSFVAMAQA ARPYLNPNAA LLTLSYLGAE 150
RAIPNYNVMC LAKASLEAAT RVMAADLGKE GIRVNAISAG PIRTLAASGI 200
KNFKKMLSTF EKTAALRRTV TIEDVGNSAA FLCSDLASGI TGEIVHVDAG 250
FSITAMGELG EE 262
Length:262
Mass (Da):28,119
Last modified:January 23, 2007 - v3
Checksum:i71CEF6189795388E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC23379.1.
PIRiB64139.
RefSeqiNP_439876.2. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC23379; AAC23379; HI_1734.
GeneIDi950535.
KEGGihin:HI1734.
PATRICi20192225. VBIHaeInf48452_1815.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC23379.1 .
PIRi B64139.
RefSeqi NP_439876.2. NC_000907.1.

3D structure databases

ProteinModelPortali P44432.
SMRi P44432. Positions 2-259.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 71421.HI1734.

Chemistry

BindingDBi P44432.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC23379 ; AAC23379 ; HI_1734 .
GeneIDi 950535.
KEGGi hin:HI1734.
PATRICi 20192225. VBIHaeInf48452_1815.

Phylogenomic databases

eggNOGi COG0623.
KOi K00208.
OMAi GISGEIM.
OrthoDBi EOG6HF644.
PhylomeDBi P44432.

Enzyme and pathway databases

UniPathwayi UPA00094 .

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR014358. Enoyl-ACP_Rdtase_NADH.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PIRSFi PIRSF000094. Enoyl-ACP_rdct. 1 hit.
PRINTSi PR00081. GDHRDH.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
  2. Cited for: ENZYME REGULATION.
  3. Cited for: ENZYME REGULATION.

Entry informationi

Entry nameiFABI_HAEIN
AccessioniPrimary (citable) accession number: P44432
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 108 of the entry and version 3 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. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi