desulfoferrodoxin; The short N-terminal domain contains four conserved Cys for binding of a ferric iron atom, and is homologous to the small protein desulforedoxin; this domain may also be responsible for dimerization. The remainder of the molecule binds a ferrous iron atom and is similar to neelaredoxin, a monomeric blue non-heme iron protein. The homolog from Treponema pallidum scores between the trusted cutoff for orthology and the noise cutoff. Although essentially a full length homolog, it lacks three of the four Cys residues in the N-terminal domain; the domain may have lost ferric binding ability but may have some conserved structural role such as dimerization, or some new function. This protein is described in some articles as rubredoxin oxidoreductase (rbo), and its gene shares an operon with the rubredoxin gene in Desulfovibrio vulgaris Hildenborough. [Energy metabolism, Electron transport]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491171272    1 MANQFEIYKCELCGNVIEVLFAGsGGPLSCCGQPMKLMADKAIDGAKEKHVPVIEANGAGCKVKVGSAPHVMEETHWIEW 80
Cdd:TIGR00320   1 MPERLQVYKCEVCGNIVEVLNAG-IGQLVCCNQPMKLMSENTTDAAKEKHVPVIEKTGNGYKVKVGSVAHPMEEKHYIQW 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 491171272   81 IEIaTADGKRYKKFLKPGDAPEADFCIPVDKVVsAREYCNLHGLWKA 127
Cdd:TIGR00320  80 IEL-IADDKVYRKFLKPGDAPEAEFLIMADKVV-AREYCNIHGHWKA 124

Desulfoferrodoxin; Desulfoferrodoxins contains two types of iron: an Fe-S4 site very similar to that found in desulforedoxin from Desulfovibrio gigas and an octahedral coordinated high-spin ferrous site most probably with nitrogen/oxygen-containing ligands. Due to this rather unusual combination of active centres, this novel protein is named desulfoferrodoxin.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491171272   44 DGAKEKHVPVIEA---NGAG----CKVKVGSAPHVMEETHWIEWIEIATADGKRYKKFLKPGDA-PEADFCIPVDK--VV 113
Cdd:pfam01880   3 DWKEEKHVPVIECpdvVKAGepfeVKVSVGKIPHPMTEEHHIAWIELYFGEEGLARAEFTPHETePEVTFTVKLKKsgKL 82

                          90
                  ....*....|....
gi 491171272  114 SAREYCNLHGLWKA 127
Cdd:pfam01880  83 YALSYCNLHGLWEN 96

desulfoferrodoxin; The short N-terminal domain contains four conserved Cys for binding of a ferric iron atom, and is homologous to the small protein desulforedoxin; this domain may also be responsible for dimerization. The remainder of the molecule binds a ferrous iron atom and is similar to neelaredoxin, a monomeric blue non-heme iron protein. The homolog from Treponema pallidum scores between the trusted cutoff for orthology and the noise cutoff. Although essentially a full length homolog, it lacks three of the four Cys residues in the N-terminal domain; the domain may have lost ferric binding ability but may have some conserved structural role such as dimerization, or some new function. This protein is described in some articles as rubredoxin oxidoreductase (rbo), and its gene shares an operon with the rubredoxin gene in Desulfovibrio vulgaris Hildenborough. [Energy metabolism, Electron transport]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491171272    1 MANQFEIYKCELCGNVIEVLFAGsGGPLSCCGQPMKLMADKAIDGAKEKHVPVIEANGAGCKVKVGSAPHVMEETHWIEW 80
Cdd:TIGR00320   1 MPERLQVYKCEVCGNIVEVLNAG-IGQLVCCNQPMKLMSENTTDAAKEKHVPVIEKTGNGYKVKVGSVAHPMEEKHYIQW 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 491171272   81 IEIaTADGKRYKKFLKPGDAPEADFCIPVDKVVsAREYCNLHGLWKA 127
Cdd:TIGR00320  80 IEL-IADDKVYRKFLKPGDAPEAEFLIMADKVV-AREYCNIHGHWKA 124

Superoxide reductase-like (SORL) domain; present in a family of mononuclear non-heme iron proteins that includes superoxide reductase and desulfoferrodoxin. Superoxide reductase-like proteins scavenge superoxide anion radicals as a defense mechanism against reactive oxygen species and are found in anaerobic bacteria and archeae, and microaerophilic Treponema pallidum. The SORL domain contains an active iron site, Fe[His4Cys(Glu)], which in the reduced state loses the glutamate ligand. Superoxide reductase (class II) forms a homotetramer with four Fe[His4Cys(Glu)] centers. Desulfoferrodoxin (class I) is a homodimeric protein, with each protomer comprised of two domains, the N-terminal desulforedoxin (DSRD) domain and C-terminal SORL domain. Each domain has a distinct iron center: the DSRD iron center I, Fe(S-Cys)4; and the SORL iron center II, Fe[His4Cys(Glu)].

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491171272  47 KEKHVPVIEANGAGC----KVKVGSAPHVMEETHWIEWIEIATADGKRYKKFLKPGDAPEADFCIPVDK--VVSAREYCN 120
Cdd:cd00524    1 EEKHVPVIEKPDSVEpfdvKVKVGSVPHPMTEEHYIEWIELYFGDEKVGRVELTPGTKPEATFTVKAPKkgKLVALSYCN 80

                 ....*.
gi 491171272 121 LHGLWK 126
Cdd:cd00524   81 LHGLWE 86

desulfoferrodoxin ferrous iron-binding domain; This domain comprises essentially the full length of neelaredoxin, a monomeric, blue, non-heme iron protein of Desulfovibrio gigas said to bind two iron atoms per monomer with identical spectral properties. Neelaredoxin was shown recently to have significant superoxide dismutase activity. This domain is also found (in a form in which the distance between the motifs H[HWYF]IXW and CN[IL]HGXW is somewhat shorter) as the C-terminal domain of desulfoferrodoxin, which is said to bind a single ferrous iron atom.The N-terminal domain of desulfoferrodoxin is described in a separate model, dfx_rbo (TIGR00320). [Energy metabolism, Electron transport]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491171272   41 KAIDGAKEKHVPVIE---ANGAGCKVKVG---SAPHVMEETHWIEWIEIaTADGKRYKKFLKPGDAPEADFCI-----PV 109
Cdd:TIGR00332   1 QTTDWGKEKHVPVIEvlrREGGVVYVKVSvgkEIPHPMEENHHIAWIEL-IFGDEVSRKPLVPGDAPFAEFASvdgpnKV 79

                          90
                  ....*....|....*...
gi 491171272  110 DK--VVSAREYCNLHGLW 125
Cdd:TIGR00332  80 EMsgKLTARSYCNIHGLW 97

Desulfoferrodoxin, N-terminal domain; Most members of this family are small (approximately 36 amino acids) proteins that from homodimeric complexes. Each subunit contains a high-spin iron atom tetrahedrally bound to four cysteinyl sulphur atoms This family has a similar fold to the rubredoxin metal binding domain. It is also found as the N-terminal domain of desulfoferrodoxin, see (pfam01880).

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 491171272    2 ANQFEIYKCELCGNVIEVLFAGsGGPLSCCGQPMKLM 38
Cdd:pfam06397   1 PEELQVYKCEVCGNIVEVLHPG-GGTLVCCGEPMKLM 36

desulfoferrodoxin FeS4 iron-binding domain; This domain is found as essentially the full length of desulforedoxin, a 37-residue homodimeric non-heme iron protein. It is also found as the N-terminal domain of desulfoferrodoxin (rbo), a homodimeric non-heme iron protein with 2 Fe atoms per monomer in different oxidation states.This domain binds the ferric rather than the ferrous Fe of desulfoferrodoxin.Neelaredoxin, a monomeric blue non-heme iron protein, lacks this domain. [Energy metabolism, Electron transport]

                          10        20        30
                  ....*....|....*....|....*....|....
gi 491171272    2 ANQFEIYKCELCGNVIEVLFAGsGGPLSCCGQPM 35
Cdd:TIGR00319   1 TNEGQVYKCEVCGNIVEVLHAG-GGQLVCCGEPM 33