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Conserved domains on  [gi|24637305|gb|AAN63648|]
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TUS-1 [Myroides odoratus DSM 2801]

Protein Classification

subclass B1 metallo-beta-lactamase( domain architecture ID 10888874)

subclass B1 metallo-beta-lactamase, similar to Myroides odoratus TUS-1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MUS_TUS_MBL-B1 cd16318
Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; ...
 24-237 3.36e-169

Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBLs Myroides odoratimimus MUS-1 and related MBLs. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


:

Pssm-ID: 293876  Cd Length: 214  Bit Score: 465.28  E-value: 3.36e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  24 LKIEPLNDHMYVYTTYQVFQGVEYSSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGL 103
Cdd:cd16318   1 LKIKQLNDNMYIYTTYQEFQGVTYSSNSMYVLTDEGVILIDTPWDKDQYEPLLEYIRSNHNKEVKWVITTHFHEDRSGGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 104 DYFNKAGAETYTYALTNEILKQRNEPQATFTFGSTKQFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIKSAEA 183
Cdd:cd16318  81 GYFNSIGAQTYTYALTNEILKERNEPQAQFSFNKEKQFTFGNEKLAVYFLGEGHSLDNTVVWFPKEEVLYGGCLIKSAEA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24637305 184 TTIGNIVDGNVEAWPTTIKAVKRKFKKAKVIIPGHDAWNQSGHLENTARILSAY 237
Cdd:cd16318 161 TTIGNIADGNVIAWPKTIEAVKQKFKNAKVIIPGHDEWDMSGHIENTERILSAY 214
 
Name Accession Description Interval E-value
MUS_TUS_MBL-B1 cd16318
Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; ...
 24-237 3.36e-169

Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBLs Myroides odoratimimus MUS-1 and related MBLs. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293876  Cd Length: 214  Bit Score: 465.28  E-value: 3.36e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  24 LKIEPLNDHMYVYTTYQVFQGVEYSSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGL 103
Cdd:cd16318   1 LKIKQLNDNMYIYTTYQEFQGVTYSSNSMYVLTDEGVILIDTPWDKDQYEPLLEYIRSNHNKEVKWVITTHFHEDRSGGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 104 DYFNKAGAETYTYALTNEILKQRNEPQATFTFGSTKQFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIKSAEA 183
Cdd:cd16318  81 GYFNSIGAQTYTYALTNEILKERNEPQAQFSFNKEKQFTFGNEKLAVYFLGEGHSLDNTVVWFPKEEVLYGGCLIKSAEA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24637305 184 TTIGNIVDGNVEAWPTTIKAVKRKFKKAKVIIPGHDAWNQSGHLENTARILSAY 237
Cdd:cd16318 161 TTIGNIADGNVIAWPKTIEAVKQKFKNAKVIIPGHDEWDMSGHIENTERILSAY 214
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 35-241 3.19e-32

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 117.10  E-value: 3.19e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  35 VYTTYQVFQGVEYSSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRrEHNKEIKWVITTHFHEDRSGGLDYFNKA-GAET 113
Cdd:COG0491   1 VYVLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALLAALA-ALGLDIKAVLLTHLHPDHVGGLAALAEAfGAPV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 114 YTYALTNEILKQRN----------EPQATFTFGSTkqFNLGKEKIEVYFLGeGHSKDNTVVWFPEEAILYGGCLIKSAEA 183
Cdd:COG0491  80 YAHAAEAEALEAPAagalfgrepvPPDRTLEDGDT--LELGGPGLEVIHTP-GHTPGHVSFYVPDEKVLFTGDALFSGGV 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24637305 184 TTIGnIVDGNVEAWPTTIKAVKRkfKKAKVIIPGHDAWNQSGHLENTARILSAYQAQK 241
Cdd:COG0491 157 GRPD-LPDGDLAQWLASLERLLA--LPPDLVIPGHGPPTTAEAIDYLEELLAALGERA 211
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 50-218 3.36e-28

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 105.71  E-value: 3.36e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305     50 NALYVVTDEGVILIDTPWDKDQyaPLVEHIRREHNKEIKWVITTHFHEDRSGGLDYFNKA-GAETYTYALTNEILKQRNE 128
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAE--DLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEApGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305    129 PQATFTFGSTK-----------QFNLGKEKIEVYFLGeGHSKDNTVVWFPEEAILYGGCLIKSAEATTIGnIVDGNVEAW 197
Cdd:smart00849  79 LLGELGAEAEPappdrtlkdgdELDLGGGELEVIHTP-GHTPGSIVLYLPEGKILFTGDLLFAGGDGRTL-VDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 24637305    198 PTTIKAVKRKFKKAKVIIPGH 218
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
48-218 4.37e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 68.55  E-value: 4.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305    48 SSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGLDYF------NKAGAETYTYALTNE 121
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELaeatdvPVIVVAEEARELLDE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305   122 ILKQRNEPQATFTFGSTK----------QFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIKSAE----ATTIG 187
Cdd:pfam00753  85 ELGLAASRLGLPGPPVVPlppdvvleegDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEigrlDLPLG 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 24637305   188 NIVDGNVEAWPTTIKAVKRKFK-KAKVIIPGH 218
Cdd:pfam00753 165 GLLVLHPSSAESSLESLLKLAKlKAAVIVPGH 196
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
42-124 5.61e-04

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 40.45  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305   42 FQGVEYSS------NAlYVVTDEGVILIDTPWdkdqyAP----LVEHIRREHN-KEIKWVITTHFHEDRSGGLDYFNKAG 110
Cdd:PRK11921  20 FHGEEYSThrgssyNS-YLIKDEKTVLIDTVW-----QPfakeFVENLKKEIDlDKIDYIVANHGEIDHSGALPELMKEI 93

                         90
                 ....*....|....*.
gi 24637305  111 AETYTYALTN--EILK 124
Cdd:PRK11921  94 PDTPIYCTKNgaKSLK 109
 
Name Accession Description Interval E-value
MUS_TUS_MBL-B1 cd16318
Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; ...
 24-237 3.36e-169

Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBLs Myroides odoratimimus MUS-1 and related MBLs. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293876  Cd Length: 214  Bit Score: 465.28  E-value: 3.36e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  24 LKIEPLNDHMYVYTTYQVFQGVEYSSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGL 103
Cdd:cd16318   1 LKIKQLNDNMYIYTTYQEFQGVTYSSNSMYVLTDEGVILIDTPWDKDQYEPLLEYIRSNHNKEVKWVITTHFHEDRSGGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 104 DYFNKAGAETYTYALTNEILKQRNEPQATFTFGSTKQFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIKSAEA 183
Cdd:cd16318  81 GYFNSIGAQTYTYALTNEILKERNEPQAQFSFNKEKQFTFGNEKLAVYFLGEGHSLDNTVVWFPKEEVLYGGCLIKSAEA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24637305 184 TTIGNIVDGNVEAWPTTIKAVKRKFKKAKVIIPGHDAWNQSGHLENTARILSAY 237
Cdd:cd16318 161 TTIGNIADGNVIAWPKTIEAVKQKFKNAKVIIPGHDEWDMSGHIENTERILSAY 214
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 24-235 9.40e-117

IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded metallo-beta-lactamases Chryseobacterium indologenes IND-1, IND-2, and IND-7, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB, Chryseobacterium gleum CGB-1, and Empedobacter brevis EBR-1. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293857  Cd Length: 212  Bit Score: 332.49  E-value: 9.40e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  24 LKIEPLNDHMYVYTTYQVFQGVEYSSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGL 103
Cdd:cd16299   1 LKIEKLNDNLYIYTTYNEFNGVKYSANAMYLVTKKGVILFDTPWDKDQYQPLLDSIRKKHNLPVIAVIATHSHEDRAGGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 104 DYFNKAGAETYTYALTNEILKQRNEPQATFTFGSTKQFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIKSAEA 183
Cdd:cd16299  81 GYFNKIGIPTYATAMTNSILKKENKPQATYLIETDKTYKIGGEKFVVYFFGEGHTADNVVVWFPKEKVLDGGCLIKSAEA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 24637305 184 TTIGNIVDGNVEAWPTTIKAVKRKFKKAKVIIPGHDAWNQSGHLENTARILS 235
Cdd:cd16299 161 TDLGYIGEANVKEWPKTIHKLKQKFKKAKVVIPGHDEWKDQGHIENTLKLLN 212
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 24-234 1.61e-90

metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 266.07  E-value: 1.61e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  24 LKIEPLNDHMYVYTTYQVFQGVEYSSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGL 103
Cdd:cd16285   1 LRIRPLADNVWVHTSLAEFNGGAVPSNGLIVIDGKGLVLIDTPWTEAQTATLLDWIEKKLGKPVTAAISTHSHDDRTGGI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 104 DYFNKAGAETYTYALTNEILKQRNEPQATFTFgsTKQFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIKSAEA 183
Cdd:cd16285  81 KALNARGIPTYATALTNELAKKEGKPVPTHSL--KGALTLGFGPLEVFYPGPGHTPDNIVVWLPKSKILFGGCLVKSASA 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 24637305 184 TTIGNIVDGNVEAWPTTIKAVKRKFKKAKVIIPGHDAWNQSGHLENTARIL 234
Cdd:cd16285 159 TSLGNVGDADVEAWPKSIENLKAKYPEARMVVPGHGAPGGTELLDHTLDLA 209
BlaB-like_MBL-B1 cd16316
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related ...
 24-237 1.48e-88

Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBL Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related MBLs. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293874  Cd Length: 214  Bit Score: 261.24  E-value: 1.48e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  24 LKIEPLNDHMYVYTTYQVFQGVEYSSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGL 103
Cdd:cd16316   1 LKISHLTGDLYVYTTYNTYKGTKTAANAVYVVTDKGVVVIDAPWDETQFQPFLDSIQKKHHKKVIMNIATHSHDDRAGGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 104 DYFNKAGAETYTYALTNEILKQRNEPQATFTFGSTKQFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIKSAEA 183
Cdd:cd16316  81 EYFGKKGAKTYTTKLTDSILKKNNKPRAEYTFDNDTTFKVGKYEFQVYYPGKGHTADNIVVWFPKEKVLYGGCLIKSADA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24637305 184 TTIGNIVDGNVEAWPTTIKAVKRKFKKAKVIIPGHDAWNQSGHLENTARILSAY 237
Cdd:cd16316 161 KDLGYLGEAYVNDWTQSIHNIQQKFPNPQYVIAGHDDWKDQTSLQHTLKLISEY 214
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 24-235 3.32e-78

Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 234.87  E-value: 3.32e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  24 LKIEPLNDHMYVYTTYQVFQGVEYSSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGL 103
Cdd:cd16304   1 LEVTKLNKNVWVHTSYGLFNGTPVPSNGLIVETSKGVVLIDTPWDDEQTEELLDWIKKKLKKPVTLAIVTHAHDDRIGGI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 104 DYFNKAGAETYTYALTNEILKQRNEPQATFTFGSTKQFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIKSAEA 183
Cdd:cd16304  81 KALQKRGIPVYSTKLTAQLAKKQGYPSPDGILKDDTTLKFGNTKIETFYPGEGHTADNIVVWLPQSKILFGGCLVKSLEA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 24637305 184 TTIGNIVDGNVEAWPTTIKAVKRKFKKAKVIIPGHDAWNQSGHLENTARILS 235
Cdd:cd16304 161 KDLGNTADANLKEWPTSIRNVLKRYPNAEIVVPGHGEWGDKQLLRHTLDLLK 212
IND_MBL-B1 cd16317
Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass ...
 28-235 5.76e-74

Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBLs Chryseobacterium indologenes IND-1, IND-2, and IND-7 and related MBLs. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293875  Cd Length: 215  Bit Score: 224.13  E-value: 5.76e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  28 PLNDHMYVYTTYQVFQGVEYSSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGLDYFN 107
Cdd:cd16317   7 PIKPNLYIYKTFGVFGGKEYSANAVYLVTKKGVVLFDVPWQKVQYQSLMDTIQKRHHLPVIAVFATHSHDDRAGDLSFYN 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 108 KAGAETYTYALTNEILKQRNEPQATFTFGSTKQFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIKSAEATTIG 187
Cdd:cd16317  87 NKGIKTYATAKTNEFLKKDGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKVLDGGCLVKSNSATDLG 166

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 24637305 188 NIVDGNVEAWPTTIKAVKRKFKKAKVIIPGHDAWNQSGHLENTARILS 235
Cdd:cd16317 167 YTGEANVEQWPKTMNKLKAKYAQATLIIPGHDEWKGGGHVEHTLDLLN 214
IMP_DIM-like_MBL-B1 cd16301
IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 22-237 1.70e-72

IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the acquired MBLs IMP-1(a beta-lactamase that is active on imipenem), DIM-1 (Dutch imipenemase), GIM-1 (German imipenemase), KHM-1 (Kyorin Health Science MBL 1), SIM-1 (Seoul imipenemase), and TMB-1 (Tripoli metallo-beta-lactamase). IMP-1, DIM-1, GIM-1, SIM-1, and TMB-1 are Class 1 integron-mediated MBLs, KMH-1 is plasmid-mediated. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of acquired MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293859 [Multi-domain]  Cd Length: 215  Bit Score: 220.23  E-value: 1.70e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  22 DKLKIEPLNDHMYVYTTYQVFQG---VeySSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRrEHNKEIKWVITTHFHED 98
Cdd:cd16301   1 PKLKIEKLSDGVYLHTSYKEVEGwglV--DANGLVVVDGKEAYLIDTPWSESDTEKLVEWIK-AQGLTLKASISTHFHED 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  99 RSGGLDYFNKAGAETYTYALTNEILKQRNEPQATFTFgSTKQFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLI 178
Cdd:cd16301  78 RTGGIGYLNSHSIPTYASELTNQLLKKNGKELATHSF-SGDEFWLLKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLV 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24637305 179 KSAEATTIGNIVDGNVEAWPTTIKAVKRKFKKAKVIIPGHDAWNQSGHLENTARILSAY 237
Cdd:cd16301 157 KSLESKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGDVSLLEHTRKLAKKA 215
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 24-235 7.20e-67

Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293860  Cd Length: 212  Bit Score: 205.94  E-value: 7.20e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  24 LKIEPLNDHMYVYTTY---QVFQGVeySSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRS 100
Cdd:cd16302   1 LEIIKLSDHVYVHVSYletETFGKV--PCNGMIVINGGEAVVFDTPTNDSQSEELIDWIENSLKAKVKAVVPTHFHDDCL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 101 GGLDYFNKAGAETYTYALTNEILKQRNEPQATFTFGSTKQFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIKS 180
Cdd:cd16302  79 GGLKAFHRRGIPSYANQKTIALAKEKGLPVPQHGFSDSLTLKLGGKKIVCRYFGEGHTKDNIVVYFPSEKVLFGGCMVKS 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24637305 181 AEAtTIGNIVDGNVEAWPTTIKAVKRKFKKAKVIIPGHDAWNQSGHLENTARILS 235
Cdd:cd16302 159 LGA-GKGNLEDANVEAWPKTVEKVKAKYPDVKIVIPGHGKIGGSELLDYTIDLFK 212
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 24-234 1.54e-53

metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B1 MBls include chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I.


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 172.34  E-value: 1.54e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  24 LKIEPLNDHMYVYTTYQvfqgvEYSSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGL 103
Cdd:cd07707   1 LSLTQINGPVWVVTDLG-----SVPSNGLVYNGSKGLVLVDSTWTPKTTKELIKEIEKVSQKPVTEVINTHFHTDRAGGN 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 104 DYFNKAGAETYTYALTNEILKQRNEPQATFTFGSTKQ----------------FNLGKEKIEVYFLGEGHSKDNTVVWFP 167
Cdd:cd07707  76 AYLKERGAKTVSTALTRDLAKSEWAEIVAFTRKGLPEypdlgyelpdgvldgdFNLQFGKVEAFYPGPAHTPDNIVVYFP 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24637305 168 EEAILYGGCLIKSAEAttiGNIVDGNVEAWPTTIKAVKRKFKKAKVIIPGHDAWNQSGHLENTARIL 234
Cdd:cd07707 156 QENVLYGGCIIKETDL---GNVADADVKEWPTSIERLKKRYRNIKAVIPGHGEVGGPELLDHTLDLL 219
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 24-218 2.15e-48

VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona integron-encoded metallo-beta-lactamase)-type MBLs are integron-associated and are widely distributed acquired MBLs. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of VIM-type MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293861 [Multi-domain]  Cd Length: 218  Bit Score: 158.87  E-value: 2.15e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  24 LKIEPLNDHMYVYTTYQVFQGVEYSSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGL 103
Cdd:cd16303   3 VRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELLLIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 104 DYFNKAGAETYTYALT------------NEILKQRNEPQATFTFGStkqfnlgkekIEVYFLGEGHSKDNTVVWFPEEAI 171
Cdd:cd16303  83 DVLRAAGVATYASPSTrrlaeaegneipTHSLEGLSSSGDAVRFGP----------VELFYPGAAHSTDNLVVYVPSARV 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 24637305 172 LYGGCLIKSAEATTIGNIVDGNVEAWPTTIKAVKRKFKKAKVIIPGH 218
Cdd:cd16303 153 LYGGCAVRELSSTSAGNVADADLAEWPTSIERIQKHYPEAEFVIPGH 199
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 24-233 6.75e-48

NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the ISCR-mediated MBLs NDM-1 (NDM (New Delhi metallo-beta-lactamase) and FIM-1 (Florence imipenemase). MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293858  Cd Length: 214  Bit Score: 157.67  E-value: 6.75e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  24 LKIEPLNDHMYVYTTYQVFQGV-EYSSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGG 102
Cdd:cd16300   1 VVFRQLAPGVWMHTSYLDMPGFgAVPSNGLIVRDGDRVLLVDTAWTDDQTAQILNWAKQELNLPVRLAVVTHAHQDKMGG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 103 LDYFNKAGAETYTYALTNEILKQRN-EP-QATFTF---GSTKQFnlgkEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCL 177
Cdd:cd16300  81 MDALHAAGIATYANALSNQLAPQEGlVPaQHSLTFaaePSTAPN----FPLKVFYPGPGHTRDNIVVGIDGTGIAFGGCL 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 24637305 178 IKSAEATTIGNIVDGNVEAWPTTIKAVKRKFKKAKVIIPGHDAWNQSGHLENTARI 233
Cdd:cd16300 157 IRPSKATSLGNLADADTEHWAASARAFGAAFPDASMIVPSHGAPDGRAAITHTARL 212
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 47-234 4.08e-40

Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; MBL-fold metallo-hydrolase domain; SPM-1 was first identified in a Pseudomonas aeruginosa strain from a paediatric leukaemia patient and is a major clinical problem. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs are most closely related to each other. SPM-1 appears to be a hybrid B1/B2 MBL.


Pssm-ID: 293844 [Multi-domain]  Cd Length: 236  Bit Score: 138.43  E-value: 4.08e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  47 YSSNALYVVTDEG-VILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGLDYFNKAGAETYTYALTNEILKQ 125
Cdd:cd16286  25 WSSNVLVVKMLDGtVVIVDSPYTNLATQTVLDWIAKTMGPRKVVAINTHFHLDGTGGNEALKKRGIPTWGSDLTKQLLLE 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 126 RNE--------------------------PQATFTFGSTKQFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIK 179
Cdd:cd16286 105 RGKadrikaaeflknedlkrriessppvpPDNVFDLKEGKVFSFGNELVEVSFPGPAHAPDNVVVYFPERKILFGGCMIK 184

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24637305 180 SAEAttIGNIVDGNVEAWPTTIKAVkRKFkKAKVIIPGHDAWNQSGHLENTARIL 234
Cdd:cd16286 185 PGKE--LGNLGDANMKAWPDSVRRL-KKF-DAKIVIPGHGERGDPGMVNKTIKVL 235
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 35-241 3.19e-32

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 117.10  E-value: 3.19e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  35 VYTTYQVFQGVEYSSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRrEHNKEIKWVITTHFHEDRSGGLDYFNKA-GAET 113
Cdd:COG0491   1 VYVLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALLAALA-ALGLDIKAVLLTHLHPDHVGGLAALAEAfGAPV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 114 YTYALTNEILKQRN----------EPQATFTFGSTkqFNLGKEKIEVYFLGeGHSKDNTVVWFPEEAILYGGCLIKSAEA 183
Cdd:COG0491  80 YAHAAEAEALEAPAagalfgrepvPPDRTLEDGDT--LELGGPGLEVIHTP-GHTPGHVSFYVPDEKVLFTGDALFSGGV 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24637305 184 TTIGnIVDGNVEAWPTTIKAVKRkfKKAKVIIPGHDAWNQSGHLENTARILSAYQAQK 241
Cdd:COG0491 157 GRPD-LPDGDLAQWLASLERLLA--LPPDLVIPGHGPPTTAEAIDYLEELLAALGERA 211
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-218 4.47e-32

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; 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.


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 116.51  E-value: 4.47e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  49 SNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGLDYFNKAGAETYTYALTNEILKQRNE 128
Cdd:cd16282  15 SNIGFIVGDDGVVVIDTGASPRLARALLAAIRKVTDKPVRYVVNTHYHGDHTLGNAAFADAGAPIIAHENTREELAARGE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 129 PQATF-------------------TFGSTKQFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIksaEATTIGNI 189
Cdd:cd16282  95 AYLELmrrlggdamagtelvlpdrTFDDGLTLDLGGRTVELIHLGPAHTPGDLVVWLPEEGVLFAGDLV---FNGRIPFL 171

                       170       180
                ....*....|....*....|....*....
gi 24637305 190 VDGNVEAWPTTIKAVKRkfKKAKVIIPGH 218
Cdd:cd16282 172 PDGSLAGWIAALDRLLA--LDATVVVPGH 198
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 50-218 3.36e-28

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 105.71  E-value: 3.36e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305     50 NALYVVTDEGVILIDTPWDKDQyaPLVEHIRREHNKEIKWVITTHFHEDRSGGLDYFNKA-GAETYTYALTNEILKQRNE 128
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAE--DLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEApGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305    129 PQATFTFGSTK-----------QFNLGKEKIEVYFLGeGHSKDNTVVWFPEEAILYGGCLIKSAEATTIGnIVDGNVEAW 197
Cdd:smart00849  79 LLGELGAEAEPappdrtlkdgdELDLGGGELEVIHTP-GHTPGSIVLYLPEGKILFTGDLLFAGGDGRTL-VDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 24637305    198 PTTIKAVKRKFKKAKVIIPGH 218
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
CphA_ImiS-like_MBL-B2 cd16306
Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, ...
 49-219 2.46e-23

Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293864  Cd Length: 222  Bit Score: 94.24  E-value: 2.46e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  49 SNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGLDYFNKAGAETYTYALTNEILKQRNE 128
Cdd:cd16306  21 ENSMVYFGAKGVTVVGATWTPDTARELHKLIKRVSRKPVLEVINTNYHTDRAGGNAYWKSIGAKVVSTRQTRDLMKSDWA 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 129 PQATFTFGSTKQ----------------FNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIKSaeatTIGNIVDG 192
Cdd:cd16306 101 EIVAFTRKGLPEypdlplvlpnvvhdgdFTLQEGKVRAFYLGPAHTPDGIFVYFPDEQVLYGNCILKE----KLGNLSFA 176

                       170       180
                ....*....|....*....|....*..
gi 24637305 193 NVEAWPTTIKAVKRKFKKAKVIIPGHD 219
Cdd:cd16306 177 DVKAYPQTLERLKAMKLPIKTVIGGHD 203
Sfh-1-like_MBL-B2 cd16305
Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold ...
 50-220 1.85e-21

Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293863  Cd Length: 226  Bit Score: 89.29  E-value: 1.85e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  50 NALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGLDYFNKAGAETYTYALTNEILKQRNEP 129
Cdd:cd16305  22 NSMVYIGTDGITIIGATWTPETAETLEKEIRKVSPLPIKEVINTNYHTDRAGGNAYWKTLGASIVSTQMTYDLEKSQWGS 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 130 QATFT------FGSTKQ----------FNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIKSaeatTIGNIVDGN 193
Cdd:cd16305 102 IVDFTrqgnnkYPNLEKslpdtvypgdFNLQNGSVRALYLGEAHTEDGIFVYFPAERVLYGNCILKE----KLGNMSFAN 177

                       170       180       190
                ....*....|....*....|....*....|.
gi 24637305 194 VEAWPTTIKAVKRKFKKAKV----IIPGHDA 220
Cdd:cd16305 178 RTEYPKTLKKLKGLIEQGELkvesIIAGHDT 208
CphS_ImiS-like_MBL-B2 cd16287
metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas ...
 50-220 6.29e-21

metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293845  Cd Length: 226  Bit Score: 87.87  E-value: 6.29e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  50 NALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGLDYFNKAGAETYTYALTNEILKQRNEP 129
Cdd:cd16287  22 NSMVYIGTDGITIIGATWTPETAETLYKEIRKVSPLPINEVINTNYHTDRAGGNAYWKTLGAKIVATQMTYDLQKSQWGS 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 130 QATFTFGSTKQ----------------FNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIKSaeatTIGNIVDGN 193
Cdd:cd16287 102 IVNFTRQGNNKypnlekslpdtvfpgdFNLQNGSIRAMYLGEAHTKDGIFVYFPAERVLYGNCILKE----NLGNMSFAN 177

                       170       180       190
                ....*....|....*....|....*....|.
gi 24637305 194 VEAWPTTIKAVK----RKFKKAKVIIPGHDA 220
Cdd:cd16287 178 RTEYPKTLEKLKglieQGELKVDSIIAGHDT 208
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-173 2.68e-20

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; 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.


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 84.94  E-value: 2.68e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  50 NALYVVTDEGVILIDTPWDKDQYapLVEHIRREHNKEIKWVITTHFHEDRSGGLDYFNKAGAETYTYALTNEILKQRNEP 129
Cdd:cd16276  11 QSMFLVTDKGVIVVDAPPSLGEN--LLAAIRKVTDKPVTHVVYSHNHADHIGGASIFKDEGATIIAHEATAELLKRNPDP 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 24637305 130 Q---ATFTFGSTKQFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILY 173
Cdd:cd16276  89 KrpvPTVTFDDEYTLEVGGQTLELSYFGPNHGPGNIVIYLPKQKVLM 135
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 47-218 7.56e-18

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; 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 which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, 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 which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 78.48  E-value: 7.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  47 YSSNAlYVVTDE--GVILIDTPWDKDQYapLVEHIRrEHNKEIKWVITTHFHEDRSGGLDYFNKA-GAETYTYALTNEIL 123
Cdd:cd06262   8 LQTNC-YLVSDEegEAILIDPGAGALEK--ILEAIE-ELGLKIKAILLTHGHFDHIGGLAELKEApGAPVYIHEADAELL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 124 KQRNEPQATFTFGSTKQ------------FNLGKEKIEVYFLGeGHSKDNTVVWFPEEAILYGGCLIKsaeATTIGNI-- 189
Cdd:cd06262  84 EDPELNLAFFGGGPLPPpepdilledgdtIELGGLELEVIHTP-GHTPGSVCFYIEEEGVLFTGDTLF---AGSIGRTdl 159

                       170       180       190
                ....*....|....*....|....*....|..
gi 24637305 190 VDGNVEawpTTIKAVKRKFKKAK---VIIPGH 218
Cdd:cd06262 160 PGGDPE---QLIESIKKLLLLLPddtVVYPGH 188
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
48-218 4.37e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 68.55  E-value: 4.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305    48 SSNALYVVTDEGVILIDTPWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGLDYF------NKAGAETYTYALTNE 121
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELaeatdvPVIVVAEEARELLDE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305   122 ILKQRNEPQATFTFGSTK----------QFNLGKEKIEVYFLGEGHSKDNTVVWFPEEAILYGGCLIKSAE----ATTIG 187
Cdd:pfam00753  85 ELGLAASRLGLPGPPVVPlppdvvleegDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEigrlDLPLG 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 24637305   188 NIVDGNVEAWPTTIKAVKRKFK-KAKVIIPGH 218
Cdd:pfam00753 165 GLLVLHPSSAESSLESLLKLAKlKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 54-218 3.43e-09

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; 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) 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.


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 54.82  E-value: 3.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  54 VVTDEGVILIDTPWDKDQYAPLVEHIRrEHNKEIKWVITTHFHEDRSGGLDYFNKA--GAETYTYALTNEILKQRNEPQA 131
Cdd:cd07739  21 IYGETEAVLVDAQFTRADAERLADWIK-ASGKTLTTIYITHGHPDHYFGLEVLLEAfpDAKVVATPAVVAHIKAQLEPKL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 132 TFTFG----------------STKQFNLGKEKIEVYFLGEGHSKDNTVVWFPEEA------ILYGGCLIKSAEATTIGNI 189
Cdd:cd07739 100 AFWGPllggnaparlvvpeplDGDTLTLEGHPLEIVGVGGGDTDDTTYLWIPSLKtvvagdVVYNGVHVWLADATTPELR 179

                       170       180
                ....*....|....*....|....*....
gi 24637305 190 vdgnvEAWPTTIKAVKRkfKKAKVIIPGH 218
Cdd:cd07739 180 -----AAWLAALDKIEA--LNPETVVPGH 201
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 45-124 2.28e-08

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; 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) 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.


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 52.53  E-value: 2.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  45 VEYSSNALYVVTDEG-VILIDTPWDKDqYAPLVEHIRREHNKEIKWVITTHFHEDRSGGLDYF-NKAGAETYTYALTNEI 122
Cdd:cd07743   4 IPGPTNIGVYVFGDKeALLIDSGLDED-AGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLqKKTGCKVYAPKIEKAF 82


                ..
gi 24637305 123 LK 124
Cdd:cd07743  83 IE 84
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 51-150 3.14e-08

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. 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.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 51.75  E-value: 3.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  51 ALYVVTDEGVILIDT-PWDKDQYAPLVEHIRREHNKEIKWVITTHFHEDRSGGLD-----------YFNKAGAETYTYAL 118
Cdd:cd07731  12 AILIQTPGKTILIDTgPRDSFGEDVVVPYLKARGIKKLDYLILTHPDADHIGGLDavlknfpvkevYMPGVTHTTKTYED 91

                        90       100       110
                ....*....|....*....|....*....|..
gi 24637305 119 TNEILKQRNEPQATFTFGstKQFNLGKEKIEV 150
Cdd:cd07731  92 LLDAIKEKGIPVTPCKAG--DRWQLGGVSFEV 121
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 45-218 1.12e-06

uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Bacillus subtilis yflN protein. 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.


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 47.60  E-value: 1.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  45 VEYSSNALYVVTDEGVILIDT--PWDkdqyAPLVEHIRREHN---KEIKWVITTHFHEDRSGGLDYFNKA-GAETYTYAL 118
Cdd:cd07721   7 LLPPVNAYLIEDDDGLTLIDTglPGS----AKRILKALRELGlspKDIRRILLTHGHIDHIGSLAALKEApGAPVYAHER 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 119 TNEILKQRNEPQATFTFGSTKQFNLGKEKIEVYFL-----GE--------------GHSKDNTVVWFPEEAILYGGCLIk 179
Cdd:cd07721  83 EAPYLEGEKPYPPPVRLGLLGLLSPLLPVKPVPVDrtledGDtldlagglrvihtpGHTPGHISLYLEEDGVLIAGDAL- 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24637305 180 saeATTIGNIVDGNVEA---WPTTIKAVKR-KFKKAKVIIPGH 218
Cdd:cd07721 162 ---VTVGGELVPPPPPFtwdMEEALESLRKlAELDPEVLAPGH 201
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 48-218 1.39e-06

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 47.87  E-value: 1.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  48 SSNAlYVVTDEGVILIDTPWDKDqYAPLVEHIRREHN-KEIKWVITTHFHEDRSGGLDYFNKA--GAETYTYALTNEILK 124
Cdd:cd07709  31 SYNS-YLIKDEKTALIDTVKEPF-FDEFLENLEEVIDpRKIDYIVVNHQEPDHSGSLPELLELapNAKIVCSKKAARFLK 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 125 QrnepqatftFGSTKQFN-----------LGKEKIEVY---FLgegHSKDNTVVWFPEEAILY----GGCLIksaeatTI 186
Cdd:cd07709 109 H---------FYPGIDERfvvvkdgdtldLGKHTLKFIpapML---HWPDTMVTYDPEDKILFsgdaFGAHG------AS 170

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 24637305 187 GNIVDGNVEAW-------------PTTiKAVKRKFKKA-----KVIIPGH 218
Cdd:cd07709 171 GELFDDEVEDYleearryyanimgPFS-KQVRKALEKLealdiKMIAPSH 219
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 39-175 2.08e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; 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.


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 47.58  E-value: 2.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  39 YQVFQGVEY---SSNALYVV-TDEGVILIDTPWDKDQYAPLVEHIRR--EHNKEIKWVITTHFHEDRSGGLDYF-NKAGA 111
Cdd:cd16280   8 FQVFDNLYYvgnKWVSAWAIdTGDGLILIDALNNNEAADLIVDGLEKlgLDPADIKYILITHGHGDHYGGAAYLkDLYGA 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 112 ETYTYALTNEILKQRNEPQATFTFGS--TK--------QFNLGKEKIEVYfLGEGHS----------KDNTVvwfPEEAI 171
Cdd:cd16280  88 KVVMSEADWDMMEEPPEEGDNPRWGPppERdivikdgdTLTLGDTTITVY-LTPGHTpgtlslifpvKDGGK---THRAG 163


                ....
gi 24637305 172 LYGG 175
Cdd:cd16280 164 LWGG 167
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 51-219 3.14e-06

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 46.82  E-value: 3.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  51 ALYVVTDEGVILIDTPWDKD---QYAPLVEHIRREHNKE----------------IKWVITTHFHEDRSGGLDYFNKAga 111
Cdd:cd07729  34 AYLIEHPEGTILVDTGFHPDaadDPGGLELAFPPGVTEEqtleeqlarlgldpedIDYVILSHLHFDHAGGLDLFPNA-- 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 112 etytyaltnEILKQRNEPQATFTFGSTKQFNLGKEKIEVYFLGEGHskdntVVWFPEEAILYGGC--------------- 176
Cdd:cd07729 112 ---------TIIVQRAELEYATGPDPLAAGYYEDVLALDDDLPGGR-----VRLVDGDYDLFPGVtliptpghtpghqsv 177

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24637305 177 LIKSAEAT---------TIGNI-------VDGNVEAWPTTIKAVKRkFKKAK--VIIPGHD 219
Cdd:cd07729 178 LVRLPEGTvllagdaayTYENLeegrppgINYDPEAALASLERLKA-LAEREgaRVIPGHD 237
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 36-220 4.75e-06

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. 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.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 45.65  E-value: 4.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  36 YTTYQVFQGVEYSSNALYVVTDEGVILIDT--PWDKDQY-APLvehirREHN---KEIKWVITTHFHEDRSGGLDYFNKA 109
Cdd:cd07711   9 YARRDSDGGFRASSTVTLIKDGGKNILVDTgtPWDRDLLlKAL-----AEHGlspEDIDYVVLTHGHPDHIGNLNLFPNA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 110 gaetytyaltnEILKQRNEPQATFTFGSTKQ---FNLGkEKIEVYFLgEGHSKDNTVVWFPEEA---ILYGGCLIKSAEA 183
Cdd:cd07711  84 -----------TVIVGWDICGDSYDDHSLEEgdgYEID-ENVEVIPT-PGHTPEDVSVLVETEKkgtVAVAGDLFEREED 150

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 24637305 184 TTIGNIVDGNVEAWPTTIKAVKRKFKKAKVIIPGHDA 220
Cdd:cd07711 151 LEDPILWDPLSEDPELQEESRKRILALADWIIPGHGP 187
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 41-150 6.47e-06

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 46.00  E-value: 6.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  41 VFQGveyssNALYVVTDEG-VILIDT--PWDKDQY-APLVEHIRREHNKEIKWVITTHFHEDRSGGLD-----------Y 105
Cdd:COG2333   8 VGQG-----DAILIRTPDGkTILIDTgpRPSFDAGeRVVLPYLRALGIRRLDLLVLTHPDADHIGGLAavleafpvgrvL 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 24637305 106 FNKAGAETYTYALTNEILKQRNEPQATFTFGSTkqFNLGKEKIEV 150
Cdd:COG2333  83 VSGPPDTSETYERLLEALKEKGIPVRPCRAGDT--WQLGGVRFEV 125
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 38-133 9.38e-06

AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Pseudomonas Aeruginosa AIM-1, Serratia marcescens SMB-1, Erythrobacter vulgaris EVM-1, and Janthinobacterium lividum THIN-B. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of AIM-1-,SMB-1-, EVM-1-, THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 45.42  E-value: 9.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  38 TYQV-FQGVeyssNALYVVTDEGVILID--TPwdkdQYAPLVE-HIRRE--HNKEIKWVITTHFHEDRSGGLDYFNKA-G 110
Cdd:cd16290  14 TYYVgTGGL----SAVLITSPQGLILIDgaLP----QSAPQIEaNIRALgfRLEDVKLILNSHAHFDHAGGIAALQRDsG 85

                        90       100
                ....*....|....*....|....*..
gi 24637305 111 AETYTYALTNEILKQ----RNEPQATF 133
Cdd:cd16290  86 ATVAASPAGAAALRSggvdPDDPQAGA 112
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 41-102 1.17e-05

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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.


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 45.18  E-value: 1.17e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24637305  41 VFQGVEYS-SNALYVVTDEGVILIDTPWDKDQYAPLVEHIRRE-HNKEIKWVITTHFHEDRSGG 102
Cdd:cd07710   9 VYQVRGYDlSNMTFIEGDTGLIIIDTLESAEAAKAALELFRKHtGDKPVKAIIYTHSHPDHFGG 72
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 61-175 1.75e-05

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. 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.


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 44.16  E-value: 1.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  61 ILIDTpwdKDQYAPLVEHIRREHNKEIKwVITTHFHEDRSGGLDYFNKAGA--------ETYTYALTNEILKQRNEPQAT 132
Cdd:cd07712  21 LLIDT---GLGIGDLKEYVRTLTDLPLL-VVATHGHFDHIGGLHEFEEVYVhpadaeilAAPDNFETLTWDAATYSVPPA 96

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 24637305 133 FTFGSTKQ---FNLGKEKIEVYFLgEGHSKDNTVVWFPEEAILYGG 175
Cdd:cd07712  97 GPTLPLRDgdvIDLGDRQLEVIHT-PGHTPGSIALLDRANRLLFSG 141
NorV COG0426
Flavorubredoxin [Energy production and conversion];
43-173 4.05e-05

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 44.05  E-value: 4.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  43 QGVEYssNAlYVVTDEGVILIDTPWDKDqYAPLVEHIRREHN-KEIKWVITTHFHEDRSGGLDYFNKA--GAETYTYALT 119
Cdd:COG0426  30 RGTTY--NS-YLIVDEKTALIDTVGESF-FEEFLENLSKVIDpKKIDYIIVNHQEPDHSGSLPELLELapNAKIVCSKKA 105

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24637305 120 NEILKQrnepqatftFGSTKQFN-----------LGKEKIEVY---FLgegHSKDNTVVWFPEEAILY 173
Cdd:COG0426 106 ARFLPH---------FYGIPDFRfivvkegdtldLGGHTLQFIpapML---HWPDTMFTYDPEDKILF 161
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 49-175 8.40e-05

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. 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.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 42.29  E-value: 8.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  49 SNALYVVTD-EGVILIDT-PWDKDQYAPLVEHIRR--EHNKEIKWVITTHFHEDRSGGLDYFNKAGAETyTYALTNEILK 124
Cdd:cd07725  14 HVNVYLLRDgDETTLIDTgLATEEDAEALWEGLKElgLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGAT-VYILDVTPVK 92

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 24637305 125 QRNepqatftfgstkQFNLGKEKIEVYFLGeGHSKDNTVVWFPEEAILYGG 175
Cdd:cd07725  93 DGD------------KIDLGGLRLKVIETP-GHTPGHIVLYDEDRRELFVG 130
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 53-177 1.91e-04

ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 40.85  E-value: 1.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  53 YVVTDEGV---ILIDTPWDK-DQYaplVEHIRrEHNKEIKWVITTHFHEDR-SGGLDYFNKAGAETYtyaltneILKQRN 127
Cdd:cd07724  15 YLVGDPETgeaAVIDPVRDSvDRY---LDLAA-ELGLKITYVLETHVHADHvSGARELAERTGAPIV-------IGEGAP 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 24637305 128 EPQATFTFGSTKQFNLGKEKIEVYFLgEGHSKDN-TVVWFPEEAILYGGCL 177
Cdd:cd07724  84 ASFFDRLLKDGDVLELGNLTLEVLHT-PGHTPESvSYLVGDPDAVFTGDTL 133
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 61-175 2.94e-04

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. 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.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 40.59  E-value: 2.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  61 ILIDTPWDKDQYAPLVEH-IRREHNKEIKWVITTHFHEDRSGGL----DYFNKAGAETYTYaLTNEILKQRNEPQATFTF 135
Cdd:cd07722  30 ILIDTGEGRPSYIPLLKSvLDSEGNATISDILLTHWHHDHVGGLpdvlDLLRGPSPRVYKF-PRPEEDEDPDEDGGDIHD 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 24637305 136 GSTKQ-FNLGKEKIEVYFLgEGHSKDNTVVWFPEEAILYGG 175
Cdd:cd07722 109 LQDGQvFKVEGATLRVIHT-PGHTTDHVCFLLEEENALFTG 148
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 53-176 4.54e-04

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 39.75  E-value: 4.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  53 YVVTDEG---VILIDTPWDKdqyaPLVEHIRrEHNKEIKWVITTHFHEDRSGG----LDYFNKA---GAETYTYALTNEI 122
Cdd:cd07723  12 YLIVDEAtgeAAVVDPGEAE----PVLAALE-KNGLTLTAILTTHHHWDHTGGnaelKALFPDApvyGPAEDRIPGLDHP 86

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24637305 123 LKQrnepqatftfGSTkqFNLGKEKIEVYFLGeGHSKDNTVVWFPEEAILY-------GGC 176
Cdd:cd07723  87 VKD----------GDE--IKLGGLEVKVLHTP-GHTLGHICYYVPDEPALFtgdtlfsGGC 134
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
42-124 5.61e-04

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 40.45  E-value: 5.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305   42 FQGVEYSS------NAlYVVTDEGVILIDTPWdkdqyAP----LVEHIRREHN-KEIKWVITTHFHEDRSGGLDYFNKAG 110
Cdd:PRK11921  20 FHGEEYSThrgssyNS-YLIKDEKTVLIDTVW-----QPfakeFVENLKKEIDlDKIDYIVANHGEIDHSGALPELMKEI 93

                         90
                 ....*....|....*.
gi 24637305  111 AETYTYALTN--EILK 124
Cdd:PRK11921  94 PDTPIYCTKNgaKSLK 109
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 54-218 1.76e-03

Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293868  Cd Length: 252  Bit Score: 38.59  E-value: 1.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305  54 VVTDEGVILIDTPWDKDqyAPLVE-HIRR-EHN-KEIKWVITTHFHEDRSGGLDYFNK-AGAETYT-----YALTNEILK 124
Cdd:cd16310  27 ITSNHGAILLDGGLEEN--AALIEqNIKAlGFKlSDIKIIINTHAHYDHAGGLAQLKAdTGAKLWAsrgdrPALEAGKHI 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24637305 125 QRNEPQ-ATFT-------FGSTKQFNLGKEKIEVYfLGEGHSKDNTV-------------VWFPeeailyggCLIKSAea 183
Cdd:cd16310 105 GDNITQpAPFPavkvdriLGDGEKIKLGDITLTAT-LTPGHTKGCTTwsttvkengrplrVVFP--------CSLSVA-- 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 24637305 184 ttiGNIVDGNvEAWPTTIKAVKRKFK-----KAKVIIPGH 218
Cdd:cd16310 174 ---GNVLVGN-KTYPTIVEDYRASFArlramKADIVLTSH 209
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 54-114 3.96e-03

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 37.69  E-value: 3.96e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24637305  54 VVTDEGVILIDTpwDKDQYAPLVE-HIRREHNK--EIKWVITTHFHEDRSGGLDYFNKA-GAETY 114
Cdd:cd16288  27 ITTPQGLILIDT--GLESSAPMIKaNIRKLGFKpsDIKILLNSHAHLDHAGGLAALKKLtGAKLM 89
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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