Cytidine monophosphate-N-acetylneuraminic acid (CMP Neu5Ac) hydroxylase family, N-terminal Rieske domain; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. CMP Neu5Ac hydroxylase is the key enzyme for the synthesis of N-glycolylneuraminic acid (NeuGc) from N-acetylneuraminic acid (Neu5Ac), NeuGc and Neu5Ac are members of a family of cell surface sugars called sialic acids. All mammals except humans have both NeuGc variants on their cell surfaces. In humans, the gene encoding CMP Neu5Ac hydroxylase has a mutation within its coding region that abolishes NeuGc production.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960719   6 QTAETLLTLSPAEVANLKEGINFFRNKTTGKEYILYKEKDHLKACKNLCKHQGGLFMKDIEDLDGRSVKCTKHNWKLDVS 85
Cdd:cd03473    1 QTAETVLSLSPEEVANLKEGINFFRNKEDGKKYIIYKSKSELKACKNQCKHQGGLFIKDIEDLDGRTVRCTKHNWKLDVS 80

                         90       100
                 ....*....|....*....|....*..
gi 548960719  86 TMKYINPPGSFCQDELVIEMDENNGLS 112
Cdd:cd03473   81 TMKYVNPPDSFCQDELVVEYDEDGGLL 107

Cytidine monophosphate-N-acetylneuraminic acid (CMP Neu5Ac) hydroxylase family, N-terminal Rieske domain; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. CMP Neu5Ac hydroxylase is the key enzyme for the synthesis of N-glycolylneuraminic acid (NeuGc) from N-acetylneuraminic acid (Neu5Ac), NeuGc and Neu5Ac are members of a family of cell surface sugars called sialic acids. All mammals except humans have both NeuGc variants on their cell surfaces. In humans, the gene encoding CMP Neu5Ac hydroxylase has a mutation within its coding region that abolishes NeuGc production.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960719   6 QTAETLLTLSPAEVANLKEGINFFRNKTTGKEYILYKEKDHLKACKNLCKHQGGLFMKDIEDLDGRSVKCTKHNWKLDVS 85
Cdd:cd03473    1 QTAETVLSLSPEEVANLKEGINFFRNKEDGKKYIIYKSKSELKACKNQCKHQGGLFIKDIEDLDGRTVRCTKHNWKLDVS 80

                         90       100
                 ....*....|....*....|....*..
gi 548960719  86 TMKYINPPGSFCQDELVIEMDENNGLS 112
Cdd:cd03473   81 TMKYVNPPDSFCQDELVVEYDEDGGLL 107

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 548960719  138 QITYLTHACMDLKLGDKRMVFDPWLIGPAFARGWwllheppsdwlerlCKADLIYISHMHSDHLSYPTLKQ 208
Cdd:pfam13483   1 EITWLGHSSFLIEGGGARILTDPFRATVGYRPPP--------------VTADLVLISHGHDDHGHPETLPG 57

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960719 162 LIGPAFARGWWLLH-------EPPSDWLERLCKADLIYISHMHSDHLSYPTLKQLSQRRPDI-PIYVGDterpvfWnLDQ 233
Cdd:cd16283   17 LTDPVFSERASPVSfggpkrlTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPPYLvPLGLKK------W-FLK 89

                         90       100
                 ....*....|....*....|
gi 548960719 234 SGVGltniNVVPFGIWQQVD 253
Cdd:cd16283   90 KGIT----NVVELDWWQSTE 105

Cytidine monophosphate-N-acetylneuraminic acid (CMP Neu5Ac) hydroxylase family, N-terminal Rieske domain; The Rieske domain is a [2Fe-2S] cluster binding domain involved in electron transfer. CMP Neu5Ac hydroxylase is the key enzyme for the synthesis of N-glycolylneuraminic acid (NeuGc) from N-acetylneuraminic acid (Neu5Ac), NeuGc and Neu5Ac are members of a family of cell surface sugars called sialic acids. All mammals except humans have both NeuGc variants on their cell surfaces. In humans, the gene encoding CMP Neu5Ac hydroxylase has a mutation within its coding region that abolishes NeuGc production.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960719   6 QTAETLLTLSPAEVANLKEGINFFRNKTTGKEYILYKEKDHLKACKNLCKHQGGLFMKDIEDLDGRSVKCTKHNWKLDVS 85
Cdd:cd03473    1 QTAETVLSLSPEEVANLKEGINFFRNKEDGKKYIIYKSKSELKACKNQCKHQGGLFIKDIEDLDGRTVRCTKHNWKLDVS 80

                         90       100
                 ....*....|....*....|....*..
gi 548960719  86 TMKYINPPGSFCQDELVIEMDENNGLS 112
Cdd:cd03473   81 TMKYVNPPDSFCQDELVVEYDEDGGLL 107

Rieske domain; a [2Fe-2S] cluster binding domain commonly found in Rieske non-heme iron oxygenase (RO) systems such as naphthalene and biphenyl dioxygenases, as well as in plant/cyanobacterial chloroplast b6f and mitochondrial cytochrome bc(1) complexes. The Rieske domain can be divided into two subdomains, with an incomplete six-stranded, antiparallel beta-barrel at one end, and an iron-sulfur cluster binding subdomain at the other. The Rieske iron-sulfur center contains a [2Fe-2S] cluster, which is involved in electron transfer, and is liganded to two histidine and two cysteine residues present in conserved sequences called Rieske motifs. In RO systems, the N-terminal Rieske domain of the alpha subunit acts as an electron shuttle that accepts electrons from a reductase or ferredoxin component and transfers them to the mononuclear iron in the alpha subunit C-terminal domain to be used for catalysis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960719  17 AEVANLKEGINFFRNKTTGKEYILYKEKDHLKACKNLCKHQGGLFMKDieDLDGRSVKCTKHNWKLDVSTMKYINPPGSF 96
Cdd:cd03467    5 GALSELPPGGGRVVVVGGGPVVVVRREGGEVYALSNRCTHQGCPLSEG--EGEDGCIVCPCHGSRFDLRTGEVVSGPAPR 82

                         90
                 ....*....|..
gi 548960719  97 CQDELVIEMDEN 108
Cdd:cd03467   83 PLPKYPVKVEGD 94

metal-dependent hydrolase; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 548960719 137 VQITYLTHACMDLKLGDKRMVFDPWLIG-PAFARgwwllhePPSDWlerlcKADLIYISHMHSDHL 201
Cdd:PRK00685   1 MKITWLGHSAFLIETGGKKILIDPFITGnPLADL-------KPEDV-----KVDYILLTHGHGDHL 54

Ferredoxin subunit of nitrite reductase or a ring-hydroxylating dioxygenase [Inorganic ion transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 548960719  35 GKEYILYKEKDHLKACKNLCKHQGGLFMKDIedLDGRSVKCTKHNWKLDVSTMKYINPPGSFC 97
Cdd:COG2146   24 GKQIAVFRTDGEVYAYDNRCPHQGAPLSEGI--VDGGVVTCPLHGARFDLRTGECLGGPATEP 84

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 548960719 177 PPSDWLERLCKADLIYISHMHSDHLSYptlkqLSQRRPDIPIYVGDT-------ERPVFWNLDQSGVgltNINVVPFGIW 249
Cdd:cd07732   65 LGGLRSEEDPSVDAVLLSHAHLDHYGL-----LNYLRPDIPVYMGEAtkrilkaLLPFFGEGDPVPR---NIRVFESGKS 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 548960719 250 QQVDkSLRFM-ILMDgvHPEMDTC-IIVEYKGHKILNTVD 287
Cdd:cd07732  137 FTIG-DFTVTpYLVD--HSAPGAYaFLIEAPGKRIFYTGD 173