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
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767914242 179 TQVIAYGQ--GSSEGLRQNVDVWLWQLEGSSVVTMGGRRLSLAPDDSLLVLAGT 230
Cdd:cd07006   14 TMVLAPGDteGGPDNRHRGSDQWLYVVSGSGEAIVEGERVALKPGSLLLIEAGE 67

3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase (HAO or 3HAO) is a non-heme iron-dependent extradiol dioxygenase that catalyzes the oxidative ring opening of 3-hydroxyanthranilate (3-HAA) in the final enzymatic step of the kynurenine biosynthetic pathway in which tryptophan is converted to quinolinate, an endogenous neurotoxin, making HAO a target for pharmacological downregulation. Quinolate is also the universal de novo precursor to the pyridine ring of nicotinamide adenine dinucleotide. The enzyme forms homodimers, with two metal binding sites per molecule. One of the bound metal ions occupies the proposed ferrous-coordinated active site, which is located in a conserved double-strand beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914242   9 AWVKENRGSFQPPVCNKLMHQE-QLKVMFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPA 87
Cdd:cd06123    1 KWIEENRHLLKPPVGNKLLWQDsDFIVMVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEPGKFKDVVIKEGEIFLLPA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767914242  88 RVPHSPQRFANTVGLVVERRRLETELDGLR------------------------------FFSSEQYRTGKP 129
Cdd:cd06123   81 RVPHSPQRPADTVGLVIERKRPPGELDGLRwycencgellhevefhcddlgtqlkpaieeFFASEELRTCKP 152

3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and eukaryotes, are the enzyme 3-hydroxyanthranilate 3,4-dioxygenase. This enzyme acts on the tryptophan metabolite 3-hydroxyanthranilate and produces 2-amino-3-carboxymuconate semialdehyde, which can rearrange spontaneously to quinolinic acid and feed into nicotinamide biosynthesis, or undergo further enzymatic degradation.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914242    5 LGVRAWVKENRGSFQPPVCNKLMHQE-QLKVMFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIF 83
Cdd:TIGR03037   1 FNFKKWIDEHKHLLKPPVGNQQIWQDsEFMVTVVGGPNARTDFHDDPGEEFFYQLKGEMYLKVTEEGKREDVPIREGDIF 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767914242   84 LLPARVPHSPQRFANTVGLVVERRRLETELDGLRFFSSE 122
Cdd:TIGR03037  81 LLPPHVPHSPQRPAGSIGLVIERKRPQGELDGFQWFCPQ 119

Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to plant pathogen Xanthomonas campestris tetracenomycin polyketide synthesis protein XcTcmJ, a protein encoded by the tcmJ gene. XcTcmJ is annotated as being involved in tetracenomycin polyketide biosynthesis. Also included is Xc5357 from a different strain of X. campestris. Structure studies show that binding of zinc induces conformational changes and serves a functional role in this cupin protein. 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
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767914242 179 TQVIAYGQ--GSSEGLRQNVDVWLWQLEGSSVVTMGGRRLSLAPDDSLLVLAGT 230
Cdd:cd07006   14 TMVLAPGDteGGPDNRHRGSDQWLYVVSGSGEAIVEGERVALKPGSLLLIEAGE 67

3-Hydroxyanthranilate-3,4-dioxygenase, cupin domain; 3-Hydroxyanthranilate-3,4-dioxygenase (HAO or 3HAO) is a non-heme iron-dependent extradiol dioxygenase that catalyzes the oxidative ring opening of 3-hydroxyanthranilate (3-HAA) in the final enzymatic step of the kynurenine biosynthetic pathway in which tryptophan is converted to quinolinate, an endogenous neurotoxin, making HAO a target for pharmacological downregulation. Quinolate is also the universal de novo precursor to the pyridine ring of nicotinamide adenine dinucleotide. The enzyme forms homodimers, with two metal binding sites per molecule. One of the bound metal ions occupies the proposed ferrous-coordinated active site, which is located in a conserved double-strand beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914242   9 AWVKENRGSFQPPVCNKLMHQE-QLKVMFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIFLLPA 87
Cdd:cd06123    1 KWIEENRHLLKPPVGNKLLWQDsDFIVMVVGGPNSRKDFHINPGEEFFYQLKGDMVLKVIEPGKFKDVVIKEGEIFLLPA 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767914242  88 RVPHSPQRFANTVGLVVERRRLETELDGLR------------------------------FFSSEQYRTGKP 129
Cdd:cd06123   81 RVPHSPQRPADTVGLVIERKRPPGELDGLRwycencgellhevefhcddlgtqlkpaieeFFASEELRTCKP 152

3-hydroxyanthranilate 3,4-dioxygenase; Members of this protein family, from both bacteria and eukaryotes, are the enzyme 3-hydroxyanthranilate 3,4-dioxygenase. This enzyme acts on the tryptophan metabolite 3-hydroxyanthranilate and produces 2-amino-3-carboxymuconate semialdehyde, which can rearrange spontaneously to quinolinic acid and feed into nicotinamide biosynthesis, or undergo further enzymatic degradation.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914242    5 LGVRAWVKENRGSFQPPVCNKLMHQE-QLKVMFIGGPNTRKDYHIEEGEEVFYQLEGDMVLRVLEQGKHRDVVIRQGEIF 83
Cdd:TIGR03037   1 FNFKKWIDEHKHLLKPPVGNQQIWQDsEFMVTVVGGPNARTDFHDDPGEEFFYQLKGEMYLKVTEEGKREDVPIREGDIF 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 767914242   84 LLPARVPHSPQRFANTVGLVVERRRLETELDGLRFFSSE 122
Cdd:TIGR03037  81 LLPPHVPHSPQRPAGSIGLVIERKRPQGELDGFQWFCPQ 119

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767914242  40 PNTRKDYHI-EEGEEVFYQLEGDMVLRVLEQGKhrdVVIRQGEIFLLPARVPHSpqrFANT 99
Cdd:cd02208    8 PGTSSPPHWhPEQDEIFYVLSGEGELTLDDGET---VELKAGDIVLIPPGVPHS---FVNT 62

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 767914242  49 EEGEEVFYQLEGDMVLRVleqgKHRDVVIRQGEIFLLPARVPHSP 93
Cdd:cd02226   41 DDEDELFLVLEGELTIDF----RDRDVTLGPGEFFVVPKGVEHRP 81

Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to plant pathogen Xanthomonas campestris tetracenomycin polyketide synthesis protein XcTcmJ, a protein encoded by the tcmJ gene. XcTcmJ is annotated as being involved in tetracenomycin polyketide biosynthesis. Also included is Xc5357 from a different strain of X. campestris. Structure studies show that binding of zinc induces conformational changes and serves a functional role in this cupin protein. 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
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767914242 179 TQVIAYGQ--GSSEGLRQNVDVWLWQLEGSSVVTMGGRRLSLAPDDSLLVLAGT 230
Cdd:cd07006   14 TMVLAPGDteGGPDNRHRGSDQWLYVVSGSGEAIVEGERVALKPGSLLLIEAGE 67

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767914242  31 QLKVMFIGgPNTRKDYHI-EEGEEVFYQLEGDMVLRVLEQgkhrDVVIRQGEIFLLPARVPHspqRFANT 99
Cdd:COG0662   28 SVKRITVP-PGAELSLHVhPHRDEFFYVLEGTGEVTIGDE----EVELKAGDSVYIPAGVPH---RLRNP 89

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767914242  46 YHIEEGEeVFYQLEGDMVLRVLEQ-GKHRDVVIRQGEIFLLPARVPHSPQ 94
Cdd:COG2140   20 WHPNAAE-WYYVLSGEARMTVQDPpGRARTVDVGPGDVVYVPPGYGHYII 68