Uncharacterized conserved protein, cupin superfamily [Function unknown];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863670  83 VLPSKCEGPLHLHDDVEEVFFMLKGQITLMIQDGdnytETVLRERDLISVPPGIYRGLFNHGEEEA-LMCVMLGTNKPEI 161
Cdd:COG3837   35 LPPGASSSPYHAHSAEEEFVYVLEGELTLRIGGE----EYVLEPGDSVGFPAGVPHRLRNRGDEPArYLVVGTRAPYPDS 110

                 ...
gi 502863670 162 PTY 164
Cdd:COG3837  111 FDY 113

Uncharacterized conserved protein, cupin superfamily [Function unknown];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863670  83 VLPSKCEGPLHLHDDVEEVFFMLKGQITLMIQDGdnytETVLRERDLISVPPGIYRGLFNHGEEEA-LMCVMLGTNKPEI 161
Cdd:COG3837   35 LPPGASSSPYHAHSAEEEFVYVLEGELTLRIGGE----EYVLEPGDSVGFPAGVPHRLRNRGDEPArYLVVGTRAPYPDS 110

                 ...
gi 502863670 162 PTY 164
Cdd:COG3837  111 FDY 113

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502863670  79 FSTMVLPSKCEGPLHLHDDVEEVFFMLKGQITLMIQDGDnytETVLRERDLISVPPGIYRGLFNHGEEEALMCV 152
Cdd:cd02208    1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDGE---TVELKAGDIVLIPPGVPHSFVNTSDEPAVFLV 71

Cupin domain protein related to quercetin dioxygenase [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863670  55 MRYIGTGATGVASDTNTVQAEHFTFSTMVLPSKCEGPLHLHDDvEEVFFMLKGQITLMIQDgdnyTETVLRERDLISVPP 134
Cdd:COG1917    1 MRLAEIALTGVSVRVLADGEDELEVVRVTFEPGARTPWHSHPG-EELIYVLEGEGEVEVGG----EEYELKPGDVVFIPP 75

                         90
                 ....*....|....*....
gi 502863670 135 GIYRGLFNHGEEEALMCVM 153
Cdd:COG1917   76 GVPHAFRNLGDEPAVLLVV 94

Uncharacterized conserved protein, RmlC-like cupin domain [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863670  44 ADFDPKYRRAQ-MRYigtgATGVAsdTNTVQAEHFTFSTMVLPSKCEGPLHLHDDVEEVFFMLKGQITLMIqdGDNYTET 122
Cdd:COG4101   18 PGLDATTAGKQgLDY----FEGIS--AETVGSTGLWMGLVTIPPGARAKAHHHGEHETAIYVLSGRAETRY--GERLEHR 89

                         90       100       110
                 ....*....|....*....|....*....|.
gi 502863670 123 V-LRERDLISVPPGIYRGLFNHGEEEALMCV 152
Cdd:COG4101   90 VvTEPGDFIFIPPGVPHQEINLSDTEPAVAV 120

Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial proteins homologous to YdbB, a Bacillus subtilis protein of unknown function. It also includes protein Nmb1881 From Neisseria meningitidis, also of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 502863670  93 HLHDDVEEVFFMLKGQITLMIQDGDnyteTVLRERDLISVPPGI 136
Cdd:cd02226   38 HKHDDEDELFLVLEGELTIDFRDRD----VTLGPGEFFVVPKGV 77

WxcM-like, C-terminal; This family includes FdtA from Aneurinibacillus thermoaerophilus, which has been characterized as a dtdp-6-deoxy-3,4-keto-hexulose isomerase. It also includes WxcM from Xanthomonas campestris (pv. campestris).

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502863670   93 HLHDDVEEVFFMLKGQITLMIQDGDNYTETVLRERDL-ISVPPGIYRGLFNHGEEEALMC 151
Cdd:pfam05523  48 HAHKKLHQFLICLSGSCDVILDDGKNKKEFLLNRPSKgLYIPPMIWREQYNFSKGAVLLV 107

quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. Bacillus subtilis quercetin 2,3-dioxygenase (QDO) is a homodimer that shows oxygenase activity with several divalent metals such as Mn2+, Co2+, Fe2+, and Cu2+, although the preferred one appears to be Mn2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which then forms a Cu2+-alkylperoxo complex which then evolves into endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, both of which are included in this alignment model. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 502863670  91 PLHLHDDVEEVFFMLKGQITLMIQDgdnyTETVLRERDLISVPPGI 136
Cdd:cd02215   46 PPHYHKRHHETFYVLEGRLQLWLDG----ESRLLTPGDFASVPPGT 87

sugar 3,4-ketoisomerase QdtA and related proteins, cupin domain; This family includes cupin domains of several bacterial proteins homologous to sugar 3,4-ketoisomerases. Thermoanaerobacterium thermosaccharolyticum QdtA catalyzes a key step in the biosynthesis of these sugars, the conversion of thymidine diphosphate (dTDP)-4-keto-6-deoxyglucose to dTDP-3-keto-6-deoxyglucose. In Aneurinibacillus thermoaerophilus, TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase (also known as FdtA) is involved in the biosynthesis of dTDP-Fucp3NAc (3-acetamido-3,6-dideoxy-alpha-d-galactose), which is part of the repeating units of the glycan chain in the S-layer. Shewanella denitrificans bifunctional ketoisomerase/N-acetyltransferase (also known as FdtD) is involved in the third and fifth steps in the production of 3-acetamido-3,6-dideoxy-alpha-d-galactose or Fuc3NAc; the C-terminal cupin domain harbors the active site responsible for the isomerization reaction. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502863670  93 HLHDDVEEVFFMLKGQITLMIQDGDNYTETVLRERD--LIsVPPGIYRGLFNHgEEEALMCVM 153
Cdd:cd20292   45 HAHKKLEQLLICLSGSCEVILDDGKEKEEFVLDSPNkgLY-IPPGVWHEMYDF-SPDAVLLVL 105

ARD/ARD' family; The two acireductone dioxygenase enzymes (ARD and ARD', previously known as E-2 and E-2') from Klebsiella pneumoniae share the same amino acid sequence, but bind different metal ions: ARD binds Ni2+, ARD' binds Fe2+. ARD and ARD' can be experimentally interconverted by removal of the bound metal ion and reconstitution with the appropriate metal ion. The two enzymes share the same substrate, 1,2-dihydroxy-3-keto-5-(methylthio)pentene, but yield different products. ARD' yields the alpha-keto precursor of methionine (and formate), thus forming part of the ubiquitous methionine salvage pathway that converts 5'-methylthioadenosine (MTA) to methionine. This pathway is responsible for the tight control of the concentration of MTA, which is a powerful inhibitor of polyamine biosynthesis and transmethylation reactions. ARD yields methylthiopropanoate, carbon monoxide and formate, and thus prevents the conversion of MTA to methionine. The role of the ARD catalyzed reaction is unclear: methylthiopropanoate is cytotoxic, and carbon monoxide can activate guanylyl cyclase, leading to increased intracellular cGMP levels. This family also contains other members, whose functions are not well characterized.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502863670   93 HLHDDvEEVFFMLKGQITLMIQD-GDNYTETVLRERDLISVPPGIYRgLFNHGEEEALMCVMLGTNKPE 160
Cdd:pfam03079  88 HLHTD-EEIRYIVEGTGYFDVRDkDDVWIRVFVEKGDLISLPAGIYH-RFTTTPDNYVKALRLFVTKPG 154

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 502863670  92 LHLHDDVEEVFFMLKGQITLMIqdgDNYTETVlRERDLISVPPGIYRGLFNHGEE 146
Cdd:cd02214   34 PHRLKGSEEVYYILEGEGTMEI---DGEPREV-GPGDAVLIPPGAVQRIENTGEE 84

Bacteroides fragilis BF4112 and related proteins, cupin domain; This family includes archaeal and bacterial proteins homologous to BF4112, a Bacteroides fragilis protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502863670  83 VLPSKCEGP-LHLHDDVEEVFFMLKGQITLMIqDGDNYTetvLRERDLISVPPGIYRGLFNHGEEE-ALMCV 152
Cdd:cd06985   20 SLPAGAAVPfVHSHKENEEIYIILKGKGEFQV-DGEVFP---VKEGSVIRVAPDGKRSWRNTSDEPlIYICI 87