Description

IPR001032 is a Leghaemoglobin-like.

<p>This entry includes plant proteins that bind oxygen through a penta- or hexa-coordinated heme iron and are required for general plant development and during nodulation. Members of this family are leghemoglobins that facilitates the diffusion of O2 to bacteroids in nodules [[cite:PUB00153679], [cite:PUB00153678]]. Other members are non-symbiotic plant hemoglobins that are expressed in specific plant tissues, and overexpressed in organs of stressed plants [[cite:PUB00055462]]. Some of these proteins have functions additional to oxygen transport, such as to modulate levels of ATP and NO [[cite:PUB00153677]]. Some may even not function as an oxygen storage or transport proteins [[cite:PUB00153680]].</p> <p>Leghaemoglobins are haem-proteins, first identified in root nodules of leguminous plants, where they are crucial for supplying sufficient oxygen to root nodule bacteria for nitrogen fixation to occur [[cite:PUB00035889], [cite:PUB00006066]]. Although leghaemoglobin and myoglobin both share a common fold, and both regulate the facilitated diffusion of oxygen, leghemoglobins regulate oxygen affinity through a mechanism different from that of myoglobin using a novel combination of haem pocket amino acids that lower the oxygen affinity [[cite:PUB00035890], [cite:PUB00035891]]. The structure of leghaemoglobins is similar to that of haemoglobins and myoglobins, although there is little sequence conservation [[cite:PUB00006066]]. The protein is largely α-helical, eight helices providing the scaffold for a well-defined haem-binding pocket [[cite:PUB00006066]]. By contrast with the tetrameric mammalian globin assembly, the plant form is monomeric [[cite:PUB00004012]].</p> <p>Globins are haem-containing proteins involved in binding and/or transporting oxygen. They belong to a very large and well studied family that is widely distributed in many organisms [[cite:PUB00035866]]. Globins have evolved from a common ancestor and can be divided into three groups: single-domain globins, and two types of chimeric globins, flavohaemoglobins and globin-coupled sensors. Bacteria have all three types of globins, while archaea lack flavohaemoglobins, and eukaryotes lack globin-coupled sensors [[cite:PUB00035865]]. Several functionally different haemoglobins can coexist in the same species. The major types of globins include:</p> <ul><li>Haemoglobin (Hb): tetramer of two alpha and two beta chains, although embryonic and foetal forms can substitute the alpha or beta chain for ones with higher oxygen affinity, such as gamma, delta, epsilon or zeta chains. Hb transports oxygen from lungs to other tissues in vertebrates [[cite:PUB00035870]]. Hb proteins are also present in unicellular organisms where they act as enzymes or sensors [[cite:PUB00035871]].</li> <li>Myoglobin (Mb): monomeric protein responsible for oxygen storage in vertebrate muscle [[cite:PUB00035872]].</li> <li>Neuroglobin: a myoglobin-like haemprotein expressed in vertebrate brain and retina, where it is involved in neuroprotection from damage due to hypoxia or ischemia [[cite:PUB00029465]]. Neuroglobin belongs to a branch of the globin family that diverged early in evolution.</li> <li>Cytoglobin: an oxygen sensor expressed in multiple tissues. Related to neuroglobin [[cite:PUB00035873]].</li> <li>Erythrocruorin: highly cooperative extracellular respiratory proteins found in annelids and arthropods that are assembled from as many as 180 subunit into hexagonal bilayers [[cite:PUB00035877]].</li> <li>Leghaemoglobin (legHb or symbiotic Hb): occurs in the root nodules of leguminous plants, where it facilitates the diffusion of oxygen to symbiotic bacteriods in order to promote nitrogen fixation.</li> <li>Non-symbiotic haemoglobin (NsHb): occurs in non-leguminous plants, and can be over-expressed in stressed plants [[cite:PUB00055462]].</li> <li>Flavohaemoglobins (FHb): chimeric, with an N-terminal globin domain and a C-terminal ferredoxin reductase-like NAD/FAD-binding domain. FHb provides protection against nitric oxide via its C-terminal domain, which transfers electrons to haem in the globin [[cite:PUB00035867]].</li> <li>Globin-coupled sensors: chimeric, with an N-terminal myoglobin-like domain and a C-terminal domain that resembles the cytoplasmic signalling domain of bacterial chemoreceptors. They bind oxygen, and act to initiate an aerotactic response or regulate gene expression [[cite:PUB00035868], [cite:PUB00035869]].</li> <li>Protoglobin: a single domain globin found in archaea that is related to the N-terminal domain of globin-coupled sensors [[cite:PUB00016016]].</li> <li>Truncated 2/2 globin: lack the first helix, giving them a 2-over-2 instead of the canonical 3-over-3 α-helical sandwich fold. Can be divided into three main groups (I, II and II) based on structural features [[cite:PUB00055463]].</li> <li>Anaerobic nitrite reductase: phytoglobin that reduces nitrite to nitric oxide (NO) under anoxic conditions [[cite:PUB00153677]].</li></ul>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 14

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: