Nitrous oxide reductase [Inorganic ion transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513903   1 LGPLHTQFDSQGHGHTSMFLANGIAKFTLGEDVVKTD-EAPYTFVEKVDTNYNIGHLVTAEGDTVSPDDNYMVALNKWSI 79
Cdd:COG4263   370 LGPLHTEFDGKGNAYTTLFLDSQVVKWNIGDAIRAYKgEKVWYVVDKLDVHYQPGHLHTSMGETKEADGKYLVALNKFSK 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513903  80 DRYAPQGPLHPQNLQLIDLKGGlgPMEMIGDTPIgIGEPHYVQIIKADKLHAIDLYQpgtdvLTMQRSEFAI-DPGQEKV 158
Cdd:COG4263   450 DRFLPVGPLLPENAQLIDISGD--KMKLVHDGPT-FGEPHDAIIVHRSKIKPKKVYD-----RDDPFFPYAVkQAKEAKV 521

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513903 159 ERNGTTVEVWMSATRSHYTPDILRVKQGDTVKLHITNTEQTRDATHGFAIANYNIQASLDPGETSNFEFVADKPGAWNFY 238
Cdd:COG4263   522 IRDGNKVRVYMTSIAPHFGPDEFEVKQGDEVTVHVTNLDQVEDLTHGFAIPGYNINMEIMPQETASVTFVADKPGVYWYY 601

                  ....*..
gi 1929513903 239 CTDFCSA 245
Cdd:COG4263   602 CTWFCHA 608

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513903 164 TVEVWMSATRSHYTPDILRVKQGDTVKLHITNTEQTRDATHGFAIANYNIQASLDPGETSNFEFVADKPGAWNFYCTDFC 243
Cdd:cd04223     1 KVEVYMTAIRSHFTPDIIEVKEGDEVTVHLTNLEQDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFC 80

                  ..
gi 1929513903 244 SA 245
Cdd:cd04223    81 SA 82

Nitrous oxide reductase [Inorganic ion transport and metabolism];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513903   1 LGPLHTQFDSQGHGHTSMFLANGIAKFTLGEDVVKTD-EAPYTFVEKVDTNYNIGHLVTAEGDTVSPDDNYMVALNKWSI 79
Cdd:COG4263   370 LGPLHTEFDGKGNAYTTLFLDSQVVKWNIGDAIRAYKgEKVWYVVDKLDVHYQPGHLHTSMGETKEADGKYLVALNKFSK 449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513903  80 DRYAPQGPLHPQNLQLIDLKGGlgPMEMIGDTPIgIGEPHYVQIIKADKLHAIDLYQpgtdvLTMQRSEFAI-DPGQEKV 158
Cdd:COG4263   450 DRFLPVGPLLPENAQLIDISGD--KMKLVHDGPT-FGEPHDAIIVHRSKIKPKKVYD-----RDDPFFPYAVkQAKEAKV 521

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513903 159 ERNGTTVEVWMSATRSHYTPDILRVKQGDTVKLHITNTEQTRDATHGFAIANYNIQASLDPGETSNFEFVADKPGAWNFY 238
Cdd:COG4263   522 IRDGNKVRVYMTSIAPHFGPDEFEVKQGDEVTVHVTNLDQVEDLTHGFAIPGYNINMEIMPQETASVTFVADKPGVYWYY 601

                  ....*..
gi 1929513903 239 CTDFCSA 245
Cdd:COG4263   602 CTWFCHA 608

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513903 164 TVEVWMSATRSHYTPDILRVKQGDTVKLHITNTEQTRDATHGFAIANYNIQASLDPGETSNFEFVADKPGAWNFYCTDFC 243
Cdd:cd04223     1 KVEVYMTAIRSHFTPDIIEVKEGDEVTVHLTNLEQDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFC 80

                  ..
gi 1929513903 244 SA 245
Cdd:cd04223    81 SA 82

Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513903 164 TVEV------WMSATRSHYTPDILRVKQGDTVKLHITNTeqtrDATHGFAIANYNIQASLDPGETSNFEFVADKPGAWNF 237
Cdd:cd13842     2 TVYVtgvqwsWTFIYPNVRTPNEIVVPAGTPVRFRVTSP----DVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTI 77

                  ....*...
gi 1929513903 238 YCTDFCSA 245
Cdd:cd13842    78 ICAEYCGL 85

Plastocyanin domain containing protein [General function prediction only];

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1929513903 166 EVWMSATRSHYTPDILRVKQGDTVKLHITNTEQTrDATHGFAIANYNIQASLDPGETSNFEFVADKPGAWNFYC 239
Cdd:COG4633    37 EVTITVDGGGYSPSRITVKAGIPVRLNFTRKDPS-GCAEEVVFPDLGISQDLPLGKTVTIEFTPLKPGEYPFTC 109

Nitrosocyanin (NC) is a mononuclear red copper protein; Nitrosocyanin (NC) is isolated from the ammonia oxidizing bacterium Nitrosomonas europaea. Nitrosocyanin exhibits remote sequence homology to classic blue copper proteins; its spectroscopic and electrochemical properties are different. The structure of NC is a trimer of single domain cupredoxins. Nitroscocyanin may mediate electron transfer. It could have a novel role as a nitric oxide dehydrogenase or a nitric oxide reductase in the oxidation of ammonia.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1929513903 178 PDILRVKQGDTVKLHITNTEQtrdATHGFAIANYNIQASLDPGETSNFEFVADKPGAWNFYC 239
Cdd:cd04215    34 PETLKVKKGDVVKITVENKSP---ISEGFSIDAFGVQEVIKAGETKTISFRADKAGAFTIWC 92

Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513903 175 HYTPDILRVKQGDTVKLHITNTEQTrdaTHGFAIANYNIQASLDPGETSNFEFVADKPGAWNFYCtDFCS 244
Cdd:pfam13473  31 GFSPSRITVPAGTPVKLEFKNKDKT---PAEFESPDLGIEKVLAPGKTSTITIPPLKPGEYDFFC-DMHM 96

The second cupredoxin domain of bacterial two domain multicopper oxidase McoN and similar proteins; This family includes bacterial two domain multicopper oxidases (2dMCOs) represented by the McoN from Nitrosomonas europaea. McoN is a trimeric type C blue copper oxidase. Each subunit houses a type 1 copper site in domain 1 and a type 2/type 3 trinuclear copper cluster at the subunit-subunit interface. The 2dMCO is proposed to be a key intermediate in the evolution of three domain MCOs. The biological function of McoN has not been characterized. Multicopper oxidases couple oxidation of substrates with reduction of dioxygen to water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513903 143 TMQRSEFAIDPGQEKVERNGTTVEVWMSATRS-HYTPdILRVKQGDTVKLHITNTeqTRDAT----HG--FAIANYN--- 212
Cdd:cd04202     5 TLVLQEWFVDPGTTPMPPEGMDFNYFTINGKSfPATP-PLVVKEGDRVRIRLINL--SMDHHpmhlHGhfFLVTATDggp 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1929513903 213 IQAS---------LDPGETSNFEFVADKPGAWNFYC 239
Cdd:cd04202    82 IPGSapwpkdtlnVAPGERYDIEFVADNPGDWMFHC 117

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1929513903 166 EVWMSATRSHYTPdILRVKQGDTVKLHITNTeqtrDATHGFAIANYNIQASLDPGETSNFEFVADKPGAWNFYCTDFC 243
Cdd:cd13917     2 DVYLVARAWQWRP-VLVLKKGKTYRLHLSSL----DVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYC 74

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929513903 169 MSATRSHYTPDILRVKQGDTVKLHITnteqTRDATHGFAIANYNIQASLDPGETSNFEFVADKPGAWNFYCTDFC 243
Cdd:cd13919    23 KLGTDDDVTSPELHLPVGRPVLFNLR----SKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELC 93

Cupredoxin domain 1 of Copper-containing nitrite reductase and two-domain laccase; Copper-containing nitrite reductase (CuNIR), which catalyzes the reduction of NO2- to NO, is the key enzyme in the denitrification process in denitrifying bacteria. CuNIR contains at least one type 1 copper center and a type 2 copper center, which serves as the active site of the enzyme. A histidine, bound to the Type 2 Cu center, is responsible for binding and reducing nitrite. A Cys-His bridge plays an important role in facilitating rapid electron transfer from the type 1 center to the type 2 center. A reduced type I blue copper protein (pseudoazurin) was found to be a specific electron transfer donor for the copper-containing NIR in bacteria Alcaligenes faecalis. The two-domain laccase (small laccase) in this family differs significantly from all laccases. It resembles two domain nitrite reductase in both sequence homology and structure similarity. It consists of two domains and forms trimers and hence resembles the quaternary structure of nitrite reductases more than that of larger laccases.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1929513903 181 LRVKQGDTVKLHITNT-EQTRDAT---HGFAIANYNIQA-SLDPGETSNFEFVADKPGAWNFYC 239
Cdd:cd04201    35 LRVREGDTVELHFSNNpSSTMPHNidfHAATGAGGGAGAtFIAPGETSTFSFKATQPGLYVYHC 98

The third cupredoxin domain of uncharacterized multicopper oxidase; Multicopper Oxidases (MCOs) are multi-domain enzymes that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs oxidize their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre which binds a dioxygen. The dioxygen, following the transfer of four electrons, is reduced to two molecules of water. These MCOs are capable of oxidizing a vast range of substrates, varying from aromatic to inorganic compounds such as metals. This subfamily of MCOs is composed of three cupredoxin domains. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929513903 180 ILRVKQGDTVKLHITNTEQTRDATH------GFAIANYNI-----QASLDPGETSNFEFVADKPGAWNFYC 239
Cdd:cd13909    50 LLEARRGETVRIEMVNNTGFPHGMHlhghhfRAILPNGALgpwrdTLLMDRGETREIAFVADNPGDWLLHC 120

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1929513903 177 TPDILRVKQGDTVKLHITnteqTRDATHGFAIANYNIQASLDPGETSNFEFVADKPGAWNFYCTDFCSA 245
Cdd:cd13914    23 TSEQLVIPADRPVYFRIT----SRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGA 87

The first cupredoxin domain of CumA like multicopper oxidase; This multicopper oxidase (MCO) subfamily includes CumA from Pseudomonas putida, which is involved in the oxidation of Mn(II). However, the cumA gene has been identified in a variety of bacterial species, including both Mn(II)-oxidizing and non-Mn(II)-oxidizing strains. Thus, the proteins in this family may catalyze the oxidation of other substrates. MCO catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water and has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513903 162 GTTVEVWMSATRshyTPD-ILRVKQGDTVKLHITNteQTRDAT----HGFAIAN------YNIQASLDPGETSNFEFVAD 230
Cdd:cd13861    17 GPTTRTWGYNGQ---VPGpELRVRQGDTLRVRLTN--RLPEPTtihwHGLRLPNamdgvpGLTQPPVPPGESFTYEFTPP 91

                  ...
gi 1929513903 231 KPG 233
Cdd:cd13861    92 DAG 94

The first Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins; CueO is a multicopper oxidase (MCO) that is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the first domain. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. FtsP does not contain any copper binding sites.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929513903 142 LTMQRSEFAIDPGqekverngTTVEVWmsATRSHYTPDILRVKQGDTVKLHITN--TEQTRDATHGF---AIANYNIQAS 216
Cdd:cd04232     5 LTAQKGETEFLPG--------KKTATW--GYNGSYLGPTIRVKKGDTVRINVTNnlDEETTVHWHGLhvpGEMDGGPHQP 74

                          90       100
                  ....*....|....*....|..
gi 1929513903 217 LDPGETSNFEFVADKPGAWNFY 238
Cdd:cd04232    75 IAPGQTWSPTFTIDQPAATLWY 96

The first cupredoxin domain of plant Ascorbate oxidase; Ascorbate oxidase catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. This multicopper oxidase (MCO) is found in cucurbitaceous plants such as pumpkin, cucumber, and melon. It can detect levels of ascorbic acid and eliminate it. The biological function of ascorbate oxidase is still not clear. Ascorbate oxidase belongs to MCO family which couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1929513903 181 LRVKQGDTVKLHITNTEQTRDAT---HG--------FAIANYNIQASLDPGETSNFEFVADKPGAWnFY 238
Cdd:cd13845    33 IRATAGDTIVVELENKLPTEGVAihwHGirqrgtpwADGTASVSQCPINPGETFTYQFVVDRPGTY-FY 100