A1ZAI5

PR
Gene name
CG5065
Protein name
Putative fatty acyl-CoA reductase CG5065
Names
Species
Drosophila melanogaster (Fruit fly)
KEGG Pathway
dme:Dmel_CG5065
EC number
1.2.1.84: With NAD(+) or NADP(+) as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-128 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for A1ZAI5

Entry ID Method Resolution Chain Position Source
AF-A1ZAI5-F1 Predicted AlphaFoldDB

No variants for A1ZAI5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1ZAI5

No associated diseases with A1ZAI5

2 regional properties for A1ZAI5

Type Name Position InterPro Accession
domain Fatty acyl-coenzyme A reductase, NAD-binding domain 130 - 400 IPR013120
domain Fatty acyl-CoA reductase, C-terminal 472 - 562 IPR033640

Functions

Description
EC Number 1.2.1.84 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
  • Peroxisome membrane ; Single-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
integral component of peroxisomal membrane The component of the peroxisomal membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
intracellular membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
peroxisomal membrane The lipid bilayer surrounding a peroxisome.
peroxisome A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.

2 GO annotations of molecular function

Name Definition
alcohol-forming fatty acyl-CoA reductase activity Catalysis of the reaction: 2 NADPH + 2 H+ + a long-chain acyl-CoA = coenzyme A + 2 NADP + a long-chain alcohol.
fatty-acyl-CoA reductase (alcohol-forming) activity Catalysis of the reaction: a very long chain fatty acyl-CoA + NADPH + H+ = a very long chain primary alcohol + NADP+ + CoA.

3 GO annotations of biological process

Name Definition
ether lipid biosynthetic process The chemical reactions and pathways resulting in the formation of ether lipids, lipids that contain (normally) one lipid alcohol in ether linkage to one of the carbon atoms (normally C-1) of glycerol.
long-chain fatty-acyl-CoA metabolic process The chemical reactions and pathways involving long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more.
wax biosynthetic process The chemical reactions and pathways resulting in the formation of wax, which includes C16 and C18 fatty acids.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSHAVANKTE TEAAPNSSLK QSAAPQPANS HDAKLLNGTL ARTNGLTHAA SVATSSSGSY
70 80 90 100 110 120
GSSSAAGSNA GSGGPTSSAS LSIAAGVASS TALPLPPSSN GLQMPYERFR ADDTSYVPIA
130 140 150 160 170 180
QFYAGRSVFI TGGTGFMGKV LVEKLLRSCP EIRNIYLLIR PKRGQEVSAR LTELLNAPLF
190 200 210 220 230 240
ESLRQEKPKE LSKVIPISGD ITSEELGISE KDQNLLCRNV SVVFHSAATV KFDEKLKLSV
250 260 270 280 290 300
TINMLGTKRL VELCHRMLSL DALIHVSTAY CNCDRTDVSE VIYAPPYNPD DIISLINWLP
310 320 330 340 350 360
EDILDQLTPR LIGKRPNTYT FTKALAEHML LKEAGNLPVA IVRPSIVTAS LNEPFAGWVD
370 380 390 400 410 420
NFNGPTGLVS ALAKGMFRTM MCEKNYVADM VPVDIVINLM IAAAWRTATR KSNNLLIYNC
430 440 450 460 470 480
CTGQRNPIIW SEFVKHAMTS VRKHPLEGCL WYPTGDLRMN RPMNTLNCIA KHFLPAYILD
490 500 510 520 530 540
GVARIMGKKP FVVNVQNKIA KAVECLEYFA TRQWRFKDDN VHALLHTLSP KDREIFVFDV
550 560 570 580 590 600
RHINWDKYVE RYVLGFREFL FKQRPESLPA SRKRMLRLYY LHQLTKLVAV LLTWRFLMSR
610 620
SKRLNDLWSS FLENALRMAR LIPFL