Hydrazine synthase alpha subunit middle domain. The crystal structure of hydrazine synthase multiprotein complex isolated from the anammox organism Kuenenia stuttgartiensis implies a two-step mechanism for hydrazine synthesis: a three-electron reduction of nitric oxide to hydroxylamine at the active site of the gamma-subunit and its subsequent condensation with ammonia, yielding hydrazine in the active centre of the alpha-subunit. The alpha-subunit consists of three domains: an N-terminal domain which includes a six-bladed beta-propeller, a middle domain binding a pentacoordinated c-type haem (haem alphaI) and a C-terminal domain which harbours a bis-histidine-coordinated c-type haem (haem alphaII). This entry represents the middle domain of subunit alpha of hydrazine synthase (HZS).

Formylglycine-generating enzyme, required for sulfatase activity, contains SUMF1/FGE domain [Posttranslational modification, protein turnover, chaperones].

Sulfatase-modifying factor enzyme 1. This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.

NPCBM/NEW2 domain. This novel putative carbohydrate binding module (NPCBM) domain is found at the N-terminus of glycosyl hydrolase family 98 proteins. This domain has also been called the NEW2 domain (Naumoff DG. Phylogenetic analysis of alpha-galactosidases of the GH27 family. Molecular Biology (Engl Transl). (2004)38:388-399.)

This novel putative carbohydrate binding module (NPCBM) domain is found at the N-terminus of glycosyl hydrolase family 98 proteins.

Crystalstructure of the paralogue of the human formylglycine generating enzyme [Homo sapiens],1Y4J_B Crystal structure of the paralogue of the human formylglycine generating enzyme [Homo sapiens]

Structureof PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],5HHA_B Structure of PvdO from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1]

ChainX, Sulfatase modifying factor 1 [Homo sapiens]

ChainX, Sulfatase modifying factor 1 [Homo sapiens],2AIJ_X Chain X, Sulfatase modifying factor 1 [Homo sapiens],2AIK_X Chain X, Sulfatase modifying factor 1 [Homo sapiens],2HI8_X Chain X, Sulfatase-modifying factor 1 [Homo sapiens],2HIB_X Chain X, Sulfatase-modifying factor 1 [Homo sapiens]

humanformylglycine generating enzyme with cysteine sulfenic acid [Homo sapiens],1Y1J_X human formylglycine generating enzyme, sulfonic acid/desulfurated form [Homo sapiens]

Inactive C-alpha-formylglycine-generating enzyme 2 OS=Bos taurus OX=9913 GN=SUMF2 PE=2 SV=1

Inactive C-alpha-formylglycine-generating enzyme 2 OS=Pongo abelii OX=9601 GN=SUMF2 PE=2 SV=1

Inactive C-alpha-formylglycine-generating enzyme 2 OS=Homo sapiens OX=9606 GN=SUMF2 PE=1 SV=2

Inactive C-alpha-formylglycine-generating enzyme 2 OS=Mus musculus OX=10090 GN=Sumf2 PE=1 SV=2

Serine/threonine-protein kinase pkn1 OS=Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC) OX=227941 GN=pkn1 PE=3 SV=1