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Conserved domains on  [gi|16130838|ref|NP_417412|]
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agmatinase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

agmatinase( domain architecture ID 10011758)

agmatinase catalyzes the formation of putrescine from agmatine

CATH:  3.40.800.10
EC:  3.5.3.11
Gene Ontology:  GO:0008783|GO:0030145|GO:0033389
PubMed:  4908780|18360740
SCOP:  4000424

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK02190 PRK02190
agmatinase; Provisional
7-306 0e+00

agmatinase; Provisional


:

Pssm-ID: 235011  Cd Length: 301  Bit Score: 566.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838    7 QYDNSLVSNAFGFLRLPMNFQPYDSDADWVITGVPFDMATSGRAGGRHGPAAIRQVSTNLAWEHNRFPWNFDMRERLNVV 86
Cdd:PRK02190   1 QADESLYSNAFSFLRRPLNFTPYLSGADWVVTGVPFDMATSGRPGARFGPAAIRQASTNLAWEDRRYPWNFDLFERLAVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   87 DCGDLVYAFGDAREMSEKLQAHAEKLLAAGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTYANGCE-FDHGT 165
Cdd:PRK02190  81 DYGDLVFDYGDAEDFPEALEAHAEKILAAGKRMLTLGGDHFITLPLLRAHAKHFGPLALVHFDAHTDTWADGGSrIDHGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  166 MFYTAPKEGLIDPNHSVQIGIRTEFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDMPVYLTFDIDCLDPAFAPGTGTP 245
Cdd:PRK02190 161 MFYHAPKEGLIDPAHSVQIGIRTEYDKDNGFTVLDARQVNDRGVDAIIAQIKQIVGDMPVYLTFDIDCLDPAFAPGTGTP 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130838  246 VIGGLTSDRAIKLVRGLKDLNIVGMDVVEVAPAYDQSEITALAAATLALEMLYIQAAKKGE 306
Cdd:PRK02190 241 VIGGLTSAQALKILRGLKGLNIVGMDVVEVAPAYDHAEITALAAATLALEMLCLQAAKKGE 301
 
Name Accession Description Interval E-value
PRK02190 PRK02190
agmatinase; Provisional
7-306 0e+00

agmatinase; Provisional


Pssm-ID: 235011  Cd Length: 301  Bit Score: 566.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838    7 QYDNSLVSNAFGFLRLPMNFQPYDSDADWVITGVPFDMATSGRAGGRHGPAAIRQVSTNLAWEHNRFPWNFDMRERLNVV 86
Cdd:PRK02190   1 QADESLYSNAFSFLRRPLNFTPYLSGADWVVTGVPFDMATSGRPGARFGPAAIRQASTNLAWEDRRYPWNFDLFERLAVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   87 DCGDLVYAFGDAREMSEKLQAHAEKLLAAGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTYANGCE-FDHGT 165
Cdd:PRK02190  81 DYGDLVFDYGDAEDFPEALEAHAEKILAAGKRMLTLGGDHFITLPLLRAHAKHFGPLALVHFDAHTDTWADGGSrIDHGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  166 MFYTAPKEGLIDPNHSVQIGIRTEFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDMPVYLTFDIDCLDPAFAPGTGTP 245
Cdd:PRK02190 161 MFYHAPKEGLIDPAHSVQIGIRTEYDKDNGFTVLDARQVNDRGVDAIIAQIKQIVGDMPVYLTFDIDCLDPAFAPGTGTP 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130838  246 VIGGLTSDRAIKLVRGLKDLNIVGMDVVEVAPAYDQSEITALAAATLALEMLYIQAAKKGE 306
Cdd:PRK02190 241 VIGGLTSAQALKILRGLKGLNIVGMDVVEVAPAYDHAEITALAAATLALEMLCLQAAKKGE 301
Agmatinase_PAH cd11592
Agmatinase-like family includes proclavaminic acid amidinohydrolase; This agmatinase subfamily ...
19-284 8.72e-144

Agmatinase-like family includes proclavaminic acid amidinohydrolase; This agmatinase subfamily contains bacterial and fungal/metazoan enzymes, including proclavaminic acid amidinohydrolase (PAH, EC 3.5.3.22) and Pseudomonas aeruginosa guanidinobutyrase (GbuA) and guanidinopropionase (GpuA). PAH hydrolyzes amidinoproclavaminate to yield proclavaminate and urea in clavulanic acid biosynthesis. Clavulanic acid is an effective inhibitor of beta-lactamases and is used in combination with amoxicillin to prevent the beta-lactam rings of the antibiotic from hydrolysis and, thus keeping the antibiotic biologically active. GbuA hydrolyzes 4-guanidinobutyrate (4-GB) into 4-aminobutyrate and urea while GpuA hydrolyzes 3-guanidinopropionate (3-GP) into beta-alanine and urea. Mutation studies show that significant variations in two active site loops in these two enzymes may be important for substrate specificity. This subfamily belongs to the ureohydrolase superfamily, which includes arginase, agmatinase, proclavaminate amidinohydrolase, and formiminoglutamase.


Pssm-ID: 212538 [Multi-domain]  Cd Length: 289  Bit Score: 406.09  E-value: 8.72e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  19 FLRLPMNFQPydSDADWVITGVPFDMATSGRAGGRHGPAAIRQVSTnLAWEHNRFpWNFDMRERLNVVDCGDLVYAFGDA 98
Cdd:cd11592   5 FMRLPYVRDL--EGADVAVVGVPFDTGVSYRPGARFGPRAIRQASR-LLRPYNPA-TGVDPFDWLKVVDCGDVPVTPGDI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  99 REMSEKLQAHAEKLLAAGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTYAN--GCEFDHGTMFYTAPKEGLI 176
Cdd:cd11592  81 EDALEQIEEAYRAILAAGPRPLTLGGDHSITLPILRALAKKHGPVALVHFDAHLDTWDPyfGEKYNHGTPFRRAVEEGLL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 177 DPNHSVQIGIRT--------EFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDMPVYLTFDIDCLDPAFAPGTGTPVIG 248
Cdd:cd11592 161 DPKRSIQIGIRGslyspddlEDDRDLGFRVITADEVDDIGLDAIIEKIRERVGDGPVYLSFDIDVLDPAFAPGTGTPEIG 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 16130838 249 GLTSDRAIKLVRGLKDLNIVGMDVVEVAPAYDQSEI 284
Cdd:cd11592 241 GLTSREALEILRGLAGLNIVGADVVEVSPPYDHAEI 276
agmatinase TIGR01230
agmatinase; Members of this family include known and predicted examples of agmatinase ...
21-299 1.50e-143

agmatinase; Members of this family include known and predicted examples of agmatinase (agmatine ureohydrolase). The seed includes members of archaea, for which no definitive agmatinase sequence has yet been made available. However, archaeal sequences are phylogenetically close to the experimentally verified B. subtilis sequence. One species of Halobacterium has been demonstrated in vitro to produce agmatine from arginine, but no putrescine from ornithine, suggesting that arginine decarboxylase and agmatinase, rather than arginase and ornithine decarboxylase, lead from Arg to polyamine biosynthesis. Note: a history of early misannotation of members of this family is detailed in PUBMED:10931887.


Pssm-ID: 273514 [Multi-domain]  Cd Length: 275  Bit Score: 405.30  E-value: 1.50e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838    21 RLPMNFQPYDSDADWVITGVPFDMATSGRAGGRHGPAAIRQVSTNLAWEHNRFPWNFDMrerLNVVDCGDLVYAFGDARE 100
Cdd:TIGR01230   1 KLFMNSNPYYEEADWVIYGIPYDATTSYRPGSRHGPNAIREASWNLEWYSNRLDRDLAM---LNVVDAGDLPLAFGDARE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   101 MSEKLQAHAEKLLAAGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTYangCEFDHGTMFYTAPKEGLIDPN- 179
Cdd:TIGR01230  78 MFEKIQEHAEEFLEEGKFPVAIGGEHSITLPVIRAMAKKFGKFAVVHFDAHTDLR---DEFDGGTLNHACPMRRVIELGl 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   180 HSVQIGIRTEFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDMPVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIK-L 258
Cdd:TIGR01230 155 NVVQFGIRSGFKEENDFARENNIQVLKREVDDVIAEVKQKVGDKPVYVTIDIDVLDPAFAPGTGTPEPGGLTSDELINfF 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 16130838   259 VRGLKDLNIVGMDVVEVAPAYDQSEITALAAATLALEMLYI 299
Cdd:TIGR01230 235 VRALKDDNVVGFDVVEVAPVYDQSEVTALTAAKIALEMLLI 275
Arginase pfam00491
Arginase family;
34-282 2.38e-111

Arginase family;


Pssm-ID: 425716 [Multi-domain]  Cd Length: 272  Bit Score: 323.31  E-value: 2.38e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838    34 DWVITGVPFDMATSGRAGGRHGPAAIRQVSTNLAWEHNRFPWNFdmrERLNVVDCGDLVYAFGDAREMSEKLQAHAEKLL 113
Cdd:pfam00491   1 DVAIIGVPFDGTGSGRPGARFGPDAIREASARLEPYSLDLGVDL---EDLKVVDLGDVPVPPGDNEEVLERIEEAVAAIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   114 AAGKRMLSFGGDHFVTLPLLRAHAKHFG-KMALVHFDAHTDT---YANGCEFDHGTMFYTAPKEGLIDPNHSVQIGIRT- 188
Cdd:pfam00491  78 KAGKLPIVLGGDHSITLGSLRAVAEHYGgPLGVIHFDAHADLrdpYTTGSGNSHGTPFRRAAEEGLLDPERIVQIGIRSv 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   189 -----EFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDMPVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIKLVRGLK 263
Cdd:pfam00491 158 dneeyEYARELGITVITMREIDELGIAAVLEEILDRLGDDPVYLSFDIDVLDPAFAPGTGTPEPGGLTYREALEILRRLA 237
                         250
                  ....*....|....*....
gi 16130838   264 DLNIVGMDVVEVAPAYDQS 282
Cdd:pfam00491 238 GLNVVGADVVEVNPPYDPS 256
SpeB COG0010
Arginase/agmatinase family enzyme [Amino acid transport and metabolism]; Arginase/agmatinase ...
30-284 1.96e-88

Arginase/agmatinase family enzyme [Amino acid transport and metabolism]; Arginase/agmatinase family enzyme is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 439781 [Multi-domain]  Cd Length: 283  Bit Score: 265.54  E-value: 1.96e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  30 DSDADWVITGVPFDMATSGRAGGRHGPAAIRQVSTNLAWEHnrfpWNFDMRERLNVVDCGDLVYAFGDAREMSEKLQAHA 109
Cdd:COG0010   8 LEEADIVLLGVPSDLGVSYRPGARFGPDAIREASLNLEPYD----PGVDPLEDLGVADLGDVEVPPGDLEETLAALAEAV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 110 EKLLAAGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTY-ANGCEFDHGTMFYTAPKEGLIDPNHSVQIGIRT 188
Cdd:COG0010  84 AELLAAGKFPIVLGGDHSITLGTIRALARAYGPLGVIHFDAHADLRdPYEGNLSHGTPLRRALEEGLLDPENVVQIGIRS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 189 ------EFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDM-PVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIKLVRG 261
Cdd:COG0010 164 ndpeefELARELGVTVFTAREIRERGLAAVLEEALERLRAGdPVYVSFDIDVLDPAFAPGVGTPEPGGLTPREALELLRA 243
                       250       260
                ....*....|....*....|....
gi 16130838 262 L-KDLNIVGMDVVEVAPAYDQSEI 284
Cdd:COG0010 244 LaASGKVVGFDIVEVNPPLDPDGR 267
 
Name Accession Description Interval E-value
PRK02190 PRK02190
agmatinase; Provisional
7-306 0e+00

agmatinase; Provisional


Pssm-ID: 235011  Cd Length: 301  Bit Score: 566.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838    7 QYDNSLVSNAFGFLRLPMNFQPYDSDADWVITGVPFDMATSGRAGGRHGPAAIRQVSTNLAWEHNRFPWNFDMRERLNVV 86
Cdd:PRK02190   1 QADESLYSNAFSFLRRPLNFTPYLSGADWVVTGVPFDMATSGRPGARFGPAAIRQASTNLAWEDRRYPWNFDLFERLAVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   87 DCGDLVYAFGDAREMSEKLQAHAEKLLAAGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTYANGCE-FDHGT 165
Cdd:PRK02190  81 DYGDLVFDYGDAEDFPEALEAHAEKILAAGKRMLTLGGDHFITLPLLRAHAKHFGPLALVHFDAHTDTWADGGSrIDHGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  166 MFYTAPKEGLIDPNHSVQIGIRTEFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDMPVYLTFDIDCLDPAFAPGTGTP 245
Cdd:PRK02190 161 MFYHAPKEGLIDPAHSVQIGIRTEYDKDNGFTVLDARQVNDRGVDAIIAQIKQIVGDMPVYLTFDIDCLDPAFAPGTGTP 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130838  246 VIGGLTSDRAIKLVRGLKDLNIVGMDVVEVAPAYDQSEITALAAATLALEMLYIQAAKKGE 306
Cdd:PRK02190 241 VIGGLTSAQALKILRGLKGLNIVGMDVVEVAPAYDHAEITALAAATLALEMLCLQAAKKGE 301
Agmatinase_PAH cd11592
Agmatinase-like family includes proclavaminic acid amidinohydrolase; This agmatinase subfamily ...
19-284 8.72e-144

Agmatinase-like family includes proclavaminic acid amidinohydrolase; This agmatinase subfamily contains bacterial and fungal/metazoan enzymes, including proclavaminic acid amidinohydrolase (PAH, EC 3.5.3.22) and Pseudomonas aeruginosa guanidinobutyrase (GbuA) and guanidinopropionase (GpuA). PAH hydrolyzes amidinoproclavaminate to yield proclavaminate and urea in clavulanic acid biosynthesis. Clavulanic acid is an effective inhibitor of beta-lactamases and is used in combination with amoxicillin to prevent the beta-lactam rings of the antibiotic from hydrolysis and, thus keeping the antibiotic biologically active. GbuA hydrolyzes 4-guanidinobutyrate (4-GB) into 4-aminobutyrate and urea while GpuA hydrolyzes 3-guanidinopropionate (3-GP) into beta-alanine and urea. Mutation studies show that significant variations in two active site loops in these two enzymes may be important for substrate specificity. This subfamily belongs to the ureohydrolase superfamily, which includes arginase, agmatinase, proclavaminate amidinohydrolase, and formiminoglutamase.


Pssm-ID: 212538 [Multi-domain]  Cd Length: 289  Bit Score: 406.09  E-value: 8.72e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  19 FLRLPMNFQPydSDADWVITGVPFDMATSGRAGGRHGPAAIRQVSTnLAWEHNRFpWNFDMRERLNVVDCGDLVYAFGDA 98
Cdd:cd11592   5 FMRLPYVRDL--EGADVAVVGVPFDTGVSYRPGARFGPRAIRQASR-LLRPYNPA-TGVDPFDWLKVVDCGDVPVTPGDI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  99 REMSEKLQAHAEKLLAAGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTYAN--GCEFDHGTMFYTAPKEGLI 176
Cdd:cd11592  81 EDALEQIEEAYRAILAAGPRPLTLGGDHSITLPILRALAKKHGPVALVHFDAHLDTWDPyfGEKYNHGTPFRRAVEEGLL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 177 DPNHSVQIGIRT--------EFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDMPVYLTFDIDCLDPAFAPGTGTPVIG 248
Cdd:cd11592 161 DPKRSIQIGIRGslyspddlEDDRDLGFRVITADEVDDIGLDAIIEKIRERVGDGPVYLSFDIDVLDPAFAPGTGTPEIG 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 16130838 249 GLTSDRAIKLVRGLKDLNIVGMDVVEVAPAYDQSEI 284
Cdd:cd11592 241 GLTSREALEILRGLAGLNIVGADVVEVSPPYDHAEI 276
agmatinase TIGR01230
agmatinase; Members of this family include known and predicted examples of agmatinase ...
21-299 1.50e-143

agmatinase; Members of this family include known and predicted examples of agmatinase (agmatine ureohydrolase). The seed includes members of archaea, for which no definitive agmatinase sequence has yet been made available. However, archaeal sequences are phylogenetically close to the experimentally verified B. subtilis sequence. One species of Halobacterium has been demonstrated in vitro to produce agmatine from arginine, but no putrescine from ornithine, suggesting that arginine decarboxylase and agmatinase, rather than arginase and ornithine decarboxylase, lead from Arg to polyamine biosynthesis. Note: a history of early misannotation of members of this family is detailed in PUBMED:10931887.


Pssm-ID: 273514 [Multi-domain]  Cd Length: 275  Bit Score: 405.30  E-value: 1.50e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838    21 RLPMNFQPYDSDADWVITGVPFDMATSGRAGGRHGPAAIRQVSTNLAWEHNRFPWNFDMrerLNVVDCGDLVYAFGDARE 100
Cdd:TIGR01230   1 KLFMNSNPYYEEADWVIYGIPYDATTSYRPGSRHGPNAIREASWNLEWYSNRLDRDLAM---LNVVDAGDLPLAFGDARE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   101 MSEKLQAHAEKLLAAGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTYangCEFDHGTMFYTAPKEGLIDPN- 179
Cdd:TIGR01230  78 MFEKIQEHAEEFLEEGKFPVAIGGEHSITLPVIRAMAKKFGKFAVVHFDAHTDLR---DEFDGGTLNHACPMRRVIELGl 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   180 HSVQIGIRTEFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDMPVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIK-L 258
Cdd:TIGR01230 155 NVVQFGIRSGFKEENDFARENNIQVLKREVDDVIAEVKQKVGDKPVYVTIDIDVLDPAFAPGTGTPEPGGLTSDELINfF 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 16130838   259 VRGLKDLNIVGMDVVEVAPAYDQSEITALAAATLALEMLYI 299
Cdd:TIGR01230 235 VRALKDDNVVGFDVVEVAPVYDQSEVTALTAAKIALEMLLI 275
Arginase pfam00491
Arginase family;
34-282 2.38e-111

Arginase family;


Pssm-ID: 425716 [Multi-domain]  Cd Length: 272  Bit Score: 323.31  E-value: 2.38e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838    34 DWVITGVPFDMATSGRAGGRHGPAAIRQVSTNLAWEHNRFPWNFdmrERLNVVDCGDLVYAFGDAREMSEKLQAHAEKLL 113
Cdd:pfam00491   1 DVAIIGVPFDGTGSGRPGARFGPDAIREASARLEPYSLDLGVDL---EDLKVVDLGDVPVPPGDNEEVLERIEEAVAAIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   114 AAGKRMLSFGGDHFVTLPLLRAHAKHFG-KMALVHFDAHTDT---YANGCEFDHGTMFYTAPKEGLIDPNHSVQIGIRT- 188
Cdd:pfam00491  78 KAGKLPIVLGGDHSITLGSLRAVAEHYGgPLGVIHFDAHADLrdpYTTGSGNSHGTPFRRAAEEGLLDPERIVQIGIRSv 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   189 -----EFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDMPVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIKLVRGLK 263
Cdd:pfam00491 158 dneeyEYARELGITVITMREIDELGIAAVLEEILDRLGDDPVYLSFDIDVLDPAFAPGTGTPEPGGLTYREALEILRRLA 237
                         250
                  ....*....|....*....
gi 16130838   264 DLNIVGMDVVEVAPAYDQS 282
Cdd:pfam00491 238 GLNVVGADVVEVNPPYDPS 256
SpeB COG0010
Arginase/agmatinase family enzyme [Amino acid transport and metabolism]; Arginase/agmatinase ...
30-284 1.96e-88

Arginase/agmatinase family enzyme [Amino acid transport and metabolism]; Arginase/agmatinase family enzyme is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 439781 [Multi-domain]  Cd Length: 283  Bit Score: 265.54  E-value: 1.96e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  30 DSDADWVITGVPFDMATSGRAGGRHGPAAIRQVSTNLAWEHnrfpWNFDMRERLNVVDCGDLVYAFGDAREMSEKLQAHA 109
Cdd:COG0010   8 LEEADIVLLGVPSDLGVSYRPGARFGPDAIREASLNLEPYD----PGVDPLEDLGVADLGDVEVPPGDLEETLAALAEAV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 110 EKLLAAGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTY-ANGCEFDHGTMFYTAPKEGLIDPNHSVQIGIRT 188
Cdd:COG0010  84 AELLAAGKFPIVLGGDHSITLGTIRALARAYGPLGVIHFDAHADLRdPYEGNLSHGTPLRRALEEGLLDPENVVQIGIRS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 189 ------EFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDM-PVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIKLVRG 261
Cdd:COG0010 164 ndpeefELARELGVTVFTAREIRERGLAAVLEEALERLRAGdPVYVSFDIDVLDPAFAPGVGTPEPGGLTPREALELLRA 243
                       250       260
                ....*....|....*....|....
gi 16130838 262 L-KDLNIVGMDVVEVAPAYDQSEI 284
Cdd:COG0010 244 LaASGKVVGFDIVEVNPPLDPDGR 267
Agmatinase-like_2 cd11593
Agmatinase and related proteins; This family includes known and predicted bacterial and ...
35-281 7.72e-75

Agmatinase and related proteins; This family includes known and predicted bacterial and archaeal agmatinase (agmatine ureohydrolase; AUH; SpeB; EC=3.5.3.11), a binuclear manganese metalloenzyme that belongs to the ureohydrolase superfamily. It is a key enzyme in the synthesis of polyamine putrescine; it catalyzes hydrolysis of agmatine to yield urea and putrescine, the precursor for biosynthesis of higher polyamines, spermidine, and spermine. As compared to E. coli where two paths to putrescine exist, via decarboxylation of an amino acid, ornithine or arginine, a single path is found in Bacillus subtilis, where polyamine synthesis starts with agmatine; the speE and speB encode spermidine synthase and agmatinase, respectively. The level of agmatinase synthesis is very low, allowing strict control on the synthesis of putrescine and therefore, of all polyamines, consistent with polyamine levels in the cell. This subfamily belongs to the ureohydrolase superfamily, which includes arginase, agmatinase, proclavaminate amidinohydrolase, and formiminoglutamase.


Pssm-ID: 212539 [Multi-domain]  Cd Length: 263  Bit Score: 230.05  E-value: 7.72e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  35 WVITGVPFDMATSGRAGGRHGPAAIRQVSTNLawEHNRFPWNFDMrERLNVVDCGDLVYAFGDAREMSEKLQAHAEKLLA 114
Cdd:cd11593   1 FVILGVPYDGTVSYRPGTRFGPAAIREASYQL--ELYSPYLDRDL-EDIPFYDLGDLTLPPGDPEKVLERIEEAVKELLD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 115 AGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTD---TYaNGCEFDHGTMFYTAPKEGLIDPnhSVQIGIRT--- 188
Cdd:cd11593  78 DGKFPIVLGGEHSITLGAVRALAEKYPDLGVLHFDAHADlrdEY-EGSKYSHACVMRRILELGGVKR--LVQVGIRSgsk 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 189 -EFD--KDNGFTVLDAcqvNDRSVDDVIAQVKQIVGDMPVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIKLVRGLKD- 264
Cdd:cd11593 155 eEFEfaKEKGVRIYTF---DDFDLGRWLDELIKVLPEKPVYISIDIDVLDPAFAPGTGTPEPGGLSWRELLDLLRALAEs 231
                       250
                ....*....|....*..
gi 16130838 265 LNIVGMDVVEVAPAYDQ 281
Cdd:cd11593 232 KNIVGFDVVELSPDYDG 248
Agmatinase-like cd09990
Agmatinase-like family; Agmatinase subfamily currently includes metalloenzymes such as ...
36-284 6.81e-71

Agmatinase-like family; Agmatinase subfamily currently includes metalloenzymes such as agmatinase, guanidinobutyrase, guanidopropionase, formimidoylglutamase and proclavaminate amidinohydrolase. Agmatinase (agmatine ureohydrolase; SpeB; EC=3.5.3.11) is the key enzyme in the synthesis of polyamine putrescine; it catalyzes hydrolysis of agmatine to yield putrescine and urea. This enzyme has been found in bacteria, archaea and eukaryotes, requiring divalent Mn and sometimes Zn, Co or Ca for activity. In mammals, the highest level of agmatinase mRNA was found in liver and kidney. However, catabolism of agmatine via agmatinase apparently is a not major path; it is mostly catabolized via diamine oxidase. Agmatinase has been shown to be down-regulated in tumor renal cells. Guanidinobutyrase (Gbh, EC=3.5.3.7) catalyzes hydrolysis of 4-guanidinobutanoate to yield 4-aminobutanoate and urea in arginine degradation pathway. Activity has been shown for purified enzyme from Arthrobacter sp. KUJ 8602. Additionally, guanidinobutyrase is able to hydrolyze D-arginine, 3-guanidinopropionate, 5-guanidinovaleriate and L-arginine with much less affinity, having divalent Zn ions for catalysis. Proclavaminate amidinohydrolase (Pah, EC 3.5.3.22) hydrolyzes amidinoproclavaminate to yield proclavaminate and urea in clavulanic acid biosynthesis. Activity has been shown for purified enzyme from Streptomyces clavuligerus. Clavulanic acid is the effective inhibitor of beta-lactamases. This acid is used in combination with the penicillin amoxicillin to prevent antibiotic's beta-lactam rings from hydrolysis, thus keeping the antibiotics biologically active.


Pssm-ID: 212516 [Multi-domain]  Cd Length: 275  Bit Score: 220.50  E-value: 6.81e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  36 VITGVPFDMATSGRAGGRHGPAAIRQVSTNLAweHNRFPWNFDMRERLNVVDCGDLVYAFGDAREMSEKLQAHAEKLLAA 115
Cdd:cd09990   2 AVLGVPFDGGSTSRPGARFGPRAIREASAGYS--TYSPDLGVDDFDDLTVVDYGDVPVDPGDIEKTFDRIREAVAEIAEA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 116 GKRMLSFGGDHFVTLPLLRAHAKHF-GKMALVHFDAHTDTYA--NGCEFDHGTMFYTAPKEGLIDPNHSVQIGIR----- 187
Cdd:cd09990  80 GAIPIVLGGDHSITYPAVRGLAERHkGKVGVIHFDAHLDTRDtdGGGELSHGTPFRRLLEDGNVDGENIVQIGIRgfwns 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 188 ---TEFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDM--PVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIKLVRGL 262
Cdd:cd09990 160 peyVEYAREQGVTVITMRDVRERGLDAVIEEALEIASDGtdAVYVSVDIDVLDPAFAPGTGTPEPGGLTPRELLDAVRAL 239
                       250       260
                ....*....|....*....|...
gi 16130838 263 -KDLNIVGMDVVEVAPAYDQSEI 284
Cdd:cd09990 240 gAEAGVVGMDIVEVSPPLDPTDI 262
Ureohydrolase cd09015
Ureohydrolase superfamily includes arginase, formiminoglutamase, agmatinase and proclavaminate ...
36-280 2.94e-61

Ureohydrolase superfamily includes arginase, formiminoglutamase, agmatinase and proclavaminate amidinohydrolase (PAH); This family, also known as arginase-like amidino hydrolase family, includes Mn-dependent enzymes: arginase (Arg, EC 3.5.3.1), formimidoylglutamase (HutG, EC 3.5.3.8 ), agmatinase (SpeB, EC 3.5.3.11), guanidinobutyrase (Gbh, EC=3.5.3.7), proclavaminate amidinohydrolase (PAH, EC 3.5.3.22) and related proteins. These enzymes catalyze hydrolysis of amide bond. They are involved in control of cellular levels of arginine and ornithine (both involved in protein biosynthesis, and production of creatine, polyamines, proline and nitric acid), in histidine and arginine degradation, and in clavulanic acid biosynthesis.


Pssm-ID: 212511 [Multi-domain]  Cd Length: 270  Bit Score: 195.73  E-value: 2.94e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  36 VITGVPFDMATSGRAGGRHGPAAIRQVSTNLAWEHN-RFPWNFDMrerLNVVDCGDLVYAFGDAREMSEKLQAHAEKLLA 114
Cdd:cd09015   1 AIIGFPYDAGCEGRPGAKFGPSAIRQALLRLALVFTgLGKTRHHH---INIYDAGDIRLEGDELEEAHEKLASVVQQVLK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 115 AGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTD--TYANGCEFDHGTMFYTAPKEGLIDPNHSVQIGIR----- 187
Cdd:cd09015  78 RGAFPVVLGGDHSIAIATLRAVARHHPDLGVINLDAHLDvnTPETDGRNSSGTPFRQLLEELQQSPKHIVCIGVRgldpg 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 188 ---TEFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDMPVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIKLVRGLKD 264
Cdd:cd09015 158 palFEYARKLGVKYVTMDEVDKLGLGGVLEQLFHYDDGDNVYLSVDVDGLDPADAPGVSTPAAGGLSYREGLPILERAGK 237
                       250
                ....*....|....*..
gi 16130838 265 LN-IVGMDVVEVAPAYD 280
Cdd:cd09015 238 TKkVMGADIVEVNPLLD 254
Agmatinase_like_1 cd11589
Agmatinase and related proteins; This family includes known and predicted bacterial agmatinase ...
37-284 3.18e-49

Agmatinase and related proteins; This family includes known and predicted bacterial agmatinase (agmatine ureohydrolase; AUH; SpeB; EC=3.5.3.11), a binuclear manganese metalloenzyme, belonging to the ureohydrolase superfamily. It is a key enzyme in the synthesis of polyamine putrescine; it catalyzes hydrolysis of agmatine to yield urea and putrescine, the precursor for biosynthesis of higher polyamines, spermidine, and spermine. Agmatinase from Deinococcus radiodurans shows approximately 33% of sequence identity to human mitochondrial agmatinase. An analysis of the evolutionary relationship among ureohydrolase superfamily enzymes indicates the pathway involving arginine decarboxylase and agmatinase evolved earlier than the arginase pathway of polyamine.


Pssm-ID: 212537  Cd Length: 274  Bit Score: 164.70  E-value: 3.18e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  37 ITGVPFDMATSGRAGGRHGPAAIRQVSTNLAWEHNRFpwNFDMRERL------NVVDCGDLVYAFGDAREMSEKLQAHAE 110
Cdd:cd11589   3 VLGVPYDMGYPFRSGARFAPRAIREASTRFARGIGGY--DDDDGGLLflgdgvRIVDCGDVDIDPTDPAGNFANIEEAVR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 111 KLLAAGKRMLSFGGDHFVTLPLLRAHAKHfGKMALVHFDAHTD--------TYANG------CEFDH-GTMfytapkegl 175
Cdd:cd11589  81 KILARGAVPVVLGGDHSVTIPVLRALDEH-GPIHVVQIDAHLDwrdevngvRYGNSspmrraSEMPHvGRI--------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 176 idpnhsVQIGIR-------TEFD--KDNGFTVLDACQVNDRSVDDVIAQVKQivgDMPVYLTFDIDCLDPAFAPGTGTPV 246
Cdd:cd11589 151 ------TQIGIRglgsarpEDFDdaRAYGSVIITAREVHRIGIEAVLDQIPD---GENYYITIDIDGLDPSIAPGVGSPS 221
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 16130838 247 IGGLTSDRAIKLVRGL-KDLNIVGMDVVEVAPAYDQSEI 284
Cdd:cd11589 222 PGGLTYDQVRDLLHGLaKKGRVVGFDLVEVAPAYDPSGI 260
Arginase_HDAC cd09987
Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily ...
99-280 6.58e-36

Arginase-like and histone-like hydrolases; Arginase-like/histone-like hydrolase superfamily includes metal-dependent enzymes that belong to Arginase-like amidino hydrolase family and histone/histone-like deacetylase class I, II, IV family, respectively. These enzymes catalyze hydrolysis of amide bond. Arginases are known to be involved in control of cellular levels of arginine and ornithine, in histidine and arginine degradation and in clavulanic acid biosynthesis. Deacetylases play a role in signal transduction through histone and/or other protein modification and can repress/activate transcription of a number of different genes. They participate in different cellular processes including cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and post-translational control of the acetyl coenzyme A synthetase. Mammalian histone deacetyases are known to be involved in progression of different tumors. Specific inhibitors of mammalian histone deacetylases are an emerging class of promising novel anticancer drugs.


Pssm-ID: 212513  Cd Length: 217  Bit Score: 128.65  E-value: 6.58e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  99 REMSEKLQAHAEKLLAAGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTD--TYANGCEFDHGTMFYTApKEGLI 176
Cdd:cd09987   8 AEAHELLAGVVVAVLKDGKVPVVLGGDHSIANGAIRAVAELHPDLGVIDVDAHHDvrTPEAFGKGNHHTPRHLL-CEPLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 177 DPNHSVQIGIRTEFDKDNGFTVLDACQVNDRSVDDV-----IAQVKQIVGDM-----PVYLTFDIDCLDPAFAPGTGTPV 246
Cdd:cd09987  87 SDVHIVSIGIRGVSNGEAGGAYARKLGVVYFSMTEVdklglGDVFEEIVSYLgdkgdNVYLSVDVDGLDPSFAPGTGTPG 166
                       170       180       190
                ....*....|....*....|....*....|....*
gi 16130838 247 IGGLTSDRAIKLVRGLKDLN-IVGMDVVEVAPAYD 280
Cdd:cd09987 167 PGGLSYREGLYITERIAKTNlVVGLDIVEVNPLLD 201
Arginase cd09989
Arginase family; This family includes arginase, also known as arginase-like amidino hydrolase ...
36-280 9.74e-36

Arginase family; This family includes arginase, also known as arginase-like amidino hydrolase family, and related proteins. Arginase is a binuclear Mn-dependent metalloenzyme and catalyzes hydrolysis of L-arginine to L-ornithine and urea (Arg, EC 3.5.3.1), the reaction being the fifth and final step in the urea cycle, providing the path for the disposal of nitrogenous compounds. Arginase controls cellular levels of arginine and ornithine which are involved in protein biosynthesis, and in production of creatine, polyamines, proline and nitric acid. In vertebrates, at least two isozymes have been identified: type I (ARG1) cytoplasmic or hepatic liver-type arginase and type II (ARG2) mitochondrial or non-hepatic arginase. Point mutations in human arginase ARG1 gene lead to hyperargininemia with consequent mental disorders, retarded development and early death. Hyperargininemia is associated with a several-fold increase in the activity of the mitochondrial arginase (ARG2), causing persistent ureagenesis in patients. ARG2 overexpression plays a critical role in the pathophysiology of cholesterol mediated endothelial dysfunction. Thus, arginase is a therapeutic target to treat asthma, erectile dysfunction, atherosclerosis and cancer.


Pssm-ID: 212515  Cd Length: 290  Bit Score: 129.92  E-value: 9.74e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  36 VITGVPFDMAtSGRAGGRHGPAAIR-----QVSTNLAWEhnrfpwnfdmrerlnVVDCGDLVYAFGDAR----------- 99
Cdd:cd09989   2 SIIGVPFDLG-AGKRGVELGPEALReagllERLEELGHD---------------VEDLGDLLVPNPEEEspfngnaknld 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 100 ---EMSEKLQAHAEKLLAAGKRMLSFGGDHFVTLPLLRAHAKHFGK-MALVHFDAHTD-----TYANG----------CE 160
Cdd:cd09989  66 evlEANEKLAEAVAEALEEGRFPLVLGGDHSIAIGTIAGVARAPYPdLGVIWIDAHADintpeTSPSGnihgmplaalLG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 161 FDHGTMFYTAPKEGLIDPNHSVQIGIR------TEFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDM--PVYLTFDID 232
Cdd:cd09989 146 EGHPELTNIGGVGPKLKPENLVYIGLRdldpgeRELIKKLGIKVFTMDEIDERGIGAVMEEALEYLKPGtdGIHVSFDVD 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 16130838 233 CLDPAFAPGTGTPVIGGLTSDRAIKLVRGL-KDLNIVGMDVVEVAPAYD 280
Cdd:cd09989 226 VLDPSIAPGTGTPVPGGLTYREAHLLLEELaETGRLVSLDIVEVNPLLD 274
Formimidoylglutamase cd09988
Formimidoylglutamase or HutE; Formimidoylglutamase (N-formimidoyl-L-glutamate ...
36-282 2.45e-31

Formimidoylglutamase or HutE; Formimidoylglutamase (N-formimidoyl-L-glutamate formimidoylhydrolase; formiminoglutamase; N-formiminoglutamate hydrolase; N-formimino-L-glutamate formiminohydrolase; HutE; EC 3.5.3.8) is a metalloenzyme that catalyzes hydrolysis of N-formimidoyl-L-glutamate to L-glutamate and formamide. This enzyme is involved in histidine degradation, requiring Mn as a cofactor while glutathione may be required for maximal activity. In Pseudomonas PAO1, mutation studies show that histidine degradation proceeds via a 'four-step' pathway if the 'five-step' route is absent and vice versa; in the four-step pathway, formiminoglutaminase (HutE, EC 3.5.3.8) directly converts formiminoglutamate (FIGLU) to L-glutamate and formamide in a single step. Formiminoglutamase has traditionally also been referred to as HutG; however, formiminoglutamase is structurally and mechanistically unrelated to N-formyl-glutamate deformylase (also called HutG). Phylogenetic analysis has suggested that HutE was acquired by horizontal gene transfer from a Ralstonia-like ancestor.


Pssm-ID: 212514 [Multi-domain]  Cd Length: 262  Bit Score: 117.62  E-value: 2.45e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  36 VITGVPFDM---ATSGRAGGRHGPAAIRQVSTNLAWEHNRFpwnfdmrerlNVVDCGDLVYAFGDAREMSEKLQAHAEKL 112
Cdd:cd09988   1 ALLGFPEDEgvrRNKGRVGAAQGPDAIRKALYNLPPGNWGL----------KIYDLGDIICDGDSLEDTQQALAEVVAEL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 113 LAAGKRMLSFGGDHFVTLPLLRAHAKHFGKM-ALVHFDAHTDTYANGCEFDHGTMFYTAPKEGLIDPNHSVQIGIRT--- 188
Cdd:cd09988  71 LKKGIIPIVIGGGHDLAYGHYRGLDKALEKKiGIINFDAHFDLRPLEEGRHSGTPFRQILEECPNNLFNYSVLGIQEyyn 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 189 ---EFD--KDNGFTVLDAcqvnDRSVDDVIAQVKQIVGDM--PVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIKLVR- 260
Cdd:cd09988 151 tqeLFDlaKELGVLYFEA----ERLLGEKILDILEAEPALrdAIYLSIDLDVISSSDAPGVSAPSPNGLSPEEACAIARy 226
                       250       260
                ....*....|....*....|...
gi 16130838 261 -GLKDlNIVGMDVVEVAPAYDQS 282
Cdd:cd09988 227 aGKSG-KVRSFDIAELNPSLDID 248
Arginase-like cd11587
Arginase types I and II and arginase-like family; This family includes arginase, also known as ...
37-281 5.52e-28

Arginase types I and II and arginase-like family; This family includes arginase, also known as arginase-like amidino hydrolase family, and related proteins, found in bacteria, archaea and eykaryotes. Arginase is a binuclear Mn-dependent metalloenzyme and catalyzes hydrolysis of L-arginine to L-ornithine and urea (Arg, EC 3.5.3.1), the reaction being the fifth and final step in the urea cycle, providing the path for the disposal of nitrogenous compounds. Arginase controls cellular levels of arginine and ornithine which are involved in protein biosynthesis, and in production of creatine, polyamines, proline and nitric acid. In vertebrates, at least two isozymes have been identified: type I cytoplasmic or hepatic liver-type arginase and type II mitochondrial or non-hepatic arginase. Point mutations in human arginase gene lead to hyperargininemia with consequent mental disorders, retarded development and early death. Arginase is a therapeutic target to treat asthma, erectile dysfunction, atherosclerosis and cancer.


Pssm-ID: 212536  Cd Length: 294  Bit Score: 109.50  E-value: 5.52e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  37 ITGVPFDMATSgRAGGRHGPAAIRQvstnlAWEHNRFPwnfdmRERLNVVDCGDLvyAFGDAREMSE-------KLQAHA 109
Cdd:cd11587   2 IIGAPFSLGQP-RGGVEHGPGALRK-----AGLLEKLK-----ELEYNYEDLGDL--PFGDYENDSEfqivrnpKSVGKA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 110 EKLLAA--------GKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTD---------------TYANGCEFDHGTM 166
Cdd:cd11587  69 SEQLAGevaevvknGRFSLVLGGDHSLAIGSISGHAQVYPDLGVIWIDAHGDintpetspsgnlhgmPLAFLLGEGKGKL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 167 FYTAPKEG--LIDPNHSVQIGIRtefDKDNG-FTVLDACQVNDRSVDDV----IAQVKQIVGDM-------PVYLTFDID 232
Cdd:cd11587 149 PDVGFSWVtpLISPENVVYIGLR---DVDPGeKYIIKTLGIKYYTMFEVdklgIGKVMEETLSYllgrkkrPIHLSFDVD 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 16130838 233 CLDPAFAPGTGTPVIGGLTSDRAIKLVRGL-KDLNIVGMDVVEVAPAYDQ 281
Cdd:cd11587 226 GLDPVFAPATGTPVVGGLSYREGLLIMEELaETGLLSGMDLVEVNPSLDK 275
hutG TIGR01227
formimidoylglutamase; Formiminoglutamase, the fourth enzyme of histidine degradation, is ...
30-280 7.87e-27

formimidoylglutamase; Formiminoglutamase, the fourth enzyme of histidine degradation, is similar to arginases and agmatinases. It is often encoded near other enzymes of the histidine degredation pathway: histidine ammonia-lyase, urocanate hydratase, and imidazolonepropionase. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273513 [Multi-domain]  Cd Length: 307  Bit Score: 106.79  E-value: 7.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838    30 DSDADWVITGVPFDMAT---SGRAGGRHGPAAIRQVSTNLawehnrfpwnFDMRERLNVVDCGDLVYAFGDAREMSEKLQ 106
Cdd:TIGR01227  32 QDEKGVALIGFPLDKGVirnKGRRGARHGPSAIRQALAHL----------GDWHVSELLYDLGDIVIHGDDLEDTQHEIA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   107 AHAEKLLAAGKRMLSFGGDH---FVTLPLLRAHAKHFGKMALVHFDAHTDTYANGCEF-DHGTMFYTAPKEGLIDPNHSV 182
Cdd:TIGR01227 102 QTAAALLADHRVPVILGGGHsiaYATFAALAQHYKGTTAIGVINFDAHFDLRATEDGGpTSGTPFRQILDECQIEDFHYA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   183 QIGIRT--------EFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVGDMP-VYLTFDIDCLDPAFAPGTGTPVIGGLTSD 253
Cdd:TIGR01227 182 VLGIRRfsntqalfDYAKKLGVRYVTDDALRPGLLPTIKDILPVFLDKVDhIYLTVDMDVLDAAHAPGVSAPAPGGLYPD 261
                         250       260
                  ....*....|....*....|....*...
gi 16130838   254 RAIKLVRGLKDL-NIVGMDVVEVAPAYD 280
Cdd:TIGR01227 262 ELLELVKRIAASdKVRGAEIAEVNPTLD 289
rocF_arginase TIGR01229
arginase; This model helps resolve arginases from known and putative agmatinases, ...
37-283 1.78e-23

arginase; This model helps resolve arginases from known and putative agmatinases, formiminoglutamases, and other related proteins of unknown specifity. The pathway from arginine to the polyamine putrescine may procede by hydrolysis to remove urea (arginase) followed by decarboxylation (ornithine decarboxylase), or by decarboxylation first (arginine decarboxylase) followed by removal of urea (agmatinase).


Pssm-ID: 162262  Cd Length: 300  Bit Score: 97.50  E-value: 1.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838    37 ITGVPFDMATsGRAGGRHGPAAIRQvsTNLAWEHNRFpwNFDMRERLNVVDCG-------DLVYAFGDAREMSEKLQAHA 109
Cdd:TIGR01229   2 IVGLPFSLGQ-PRRGVDKGPSRLRE--AGLLETLRDL--EYDMQDLGQLPFAVrpkesprYAVKNPRYVLAATEQLAPKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   110 EKLLAAGKRMLSFGGDHFVTLPLLRAHAKHF--GKMALVHFDAHTDT------------------YANGCEFDHGTMFYT 169
Cdd:TIGR01229  77 YEVFEEGRFPLVLGGDHSIAIGTISGTARVHpdKKLGVLWLDAHADIntpetsdsgnihgmplafLLGRLKSEFPDSPGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   170 APKEGLIDPNHSVQIGIRT------EFDKDNGFTVLDACQVNDRSVDDVIAQVKQIVG--DMPVYLTFDIDCLDPAFAPG 241
Cdd:TIGR01229 157 GWVAPEISPKNLVYIGLRSvdpgerKILKELGIKVFSMHEIDELGIGKVVEETLEYLKaeDGPIHLSLDVDGLDPSLAPA 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 16130838   242 TGTPVIGGLTSDRAIKLVRGLKDL-NIVGMDVVEVAPAYDQSE 283
Cdd:TIGR01229 237 TGTPVVGGLTFREGLLIMEMLYESgLLTALDVVEVNPTLDIKH 279
PLN02615 PLN02615
arginase
39-280 1.95e-16

arginase


Pssm-ID: 178224  Cd Length: 338  Bit Score: 78.36  E-value: 1.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   39 GVPFDMATSGRAGGRHGPAAIRQV----STNLAWEHNRfpwnfDMRERLNVVDCGDLVY------AFGDAREM-----SE 103
Cdd:PLN02615  65 GVPLGHNSSFLQGPAFAPPRIREAiwcgSTNSTTEEGK-----ELNDPRVLTDVGDVPVqeirdcGVDDDRLMnviseSV 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  104 KLQAHAEKLlaagkRMLSFGGDHFVTLPLLRAHAKHFG-KMALVHFDAHTDTYA--NGCEFDHGTMFYTAPKEGLidPNH 180
Cdd:PLN02615 140 KLVMEEEPL-----RPLVLGGDHSISYPVVRAVSEKLGgPVDILHLDAHPDIYHafEGNKYSHASSFARIMEGGY--ARR 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  181 SVQIGIR--TEFDKDNG--FTVlDACQVNDRSVD-DVIAQVKQIVGDMPVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRA 255
Cdd:PLN02615 213 LLQVGIRsiTKEGREQGkrFGV-EQYEMRTFSKDrEKLENLKLGEGVKGVYISIDVDCLDPAFAPGVSHIEPGGLSFRDV 291
                        250       260
                 ....*....|....*....|....*
gi 16130838  256 IKLVRGLKDlNIVGMDVVEVAPAYD 280
Cdd:PLN02615 292 LNILHNLQG-DVVGADVVEFNPQRD 315
Arginase-like_1 cd09999
Arginase-like amidino hydrolase family; This family includes arginase, also known as ...
92-284 3.76e-16

Arginase-like amidino hydrolase family; This family includes arginase, also known as arginase-like amidino hydrolase family, as well as arginase-like proteins and are found in bacteria, archaea and eykaryotes, but does not include metazoan arginases. Arginase is a binuclear Mn-dependent metalloenzyme and catalyzes hydrolysis of L-arginine to L-ornithine and urea (Arg, EC 3.5.3.1), the reaction being the fifth and final step in the urea cycle, providing the path for the disposal of nitrogenous compounds. Arginase controls cellular levels of arginine and ornithine which are involved in protein biosynthesis, and in production of creatine, polyamines, proline and nitric acid.


Pssm-ID: 212523  Cd Length: 272  Bit Score: 76.90  E-value: 3.76e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  92 VYAFGDAREMSEKLQAHAEKLLAagKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTD-----TYANGcEFD---- 162
Cdd:cd09999  54 IIGRSALLAQLRAAADIIEAALP--DRPVVLGGDCSVSLAPFAYLARKYGDLGLLWIDAHPDfntpeTSPTG-YAHgmvl 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838 163 -----HGTMFYTAPKEGLIDPNHSVQIGIR------TEFDKDNGFTVLDACQVNDrSVDDVIAQVKQiVGDMPVYLTFDI 231
Cdd:cd09999 131 aallgEGDPELTAIVKPPLSPERVVLAGLRdpddeeEEFIARLGIRVLRPEGLAA-SAQAVLDWLKE-EGLSGVWIHLDL 208
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 16130838 232 DCLDPAFAPGTGTPVIGGLTSDRAIKLVRGL-KDLNIVGMDVVEVAPAYDQSEI 284
Cdd:cd09999 209 DVLDPAIFPAVDFPEPGGLSLDELVALLAALaASADLVGLTIAEFDPDLDWDAI 262
PRK13773 PRK13773
formimidoylglutamase; Provisional
48-280 4.67e-12

formimidoylglutamase; Provisional


Pssm-ID: 237499  Cd Length: 324  Bit Score: 65.54  E-value: 4.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   48 GRAGGRHGPAAIRQVSTNLAWEHNRfpwnfdmrerlNVVDCGDLVYAFGDAREMSEKLQAHAEKLLAAGKRMLSFGGDH- 126
Cdd:PRK13773  62 GRVGAAAGPDALRGALGSLALHEPR-----------RVYDAGTVTVPGGDLEAGQERLGDAVSALLDAGHLPVVLGGGHe 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  127 --FVT-LPLLRAHAKHFGK-MALVHFDAHTDTYANGcEFDHGTMF---YTAPKEGLIDPNHSVqIGI------RTEFD-- 191
Cdd:PRK13773 131 taFGSyLGVAGSERRRPGKrLGILNLDAHFDLRAAP-VPSSGTPFrqiARAEEAAGRTFQYSV-LGIsepnntRALFDta 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  192 KDNGFTVL--DACQVNDRS-----VDDVIAQVKqivgdmPVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIKLVRGLK- 263
Cdd:PRK13773 209 RELGVRYLldEECQVMDRAavrvfVADFLADVD------VIYLTIDLDVLPAAVAPGVSAPAAYGVPLEVIQAVCDRVAa 282
                        250
                 ....*....|....*....
gi 16130838  264 --DLNIVgmDVVEVAPAYD 280
Cdd:PRK13773 283 sgKLALV--DVAELNPRFD 299
PRK13775 PRK13775
formimidoylglutamase; Provisional
25-280 1.93e-10

formimidoylglutamase; Provisional


Pssm-ID: 172313 [Multi-domain]  Cd Length: 328  Bit Score: 60.76  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838   25 NFQPYDSdADWVITGVPFDMAT---SGRAGGRHGPAAIRqvsTNLAwehnRFPWNfdMRERLNVVDCGDLVyafGDAREM 101
Cdd:PRK13775  39 SLTPFEG-THFALIGFKSDKGVyinNGRVGAVESPAAIR---TQLA----KFPWH--LGNQVMVYDVGNID---GPNRSL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  102 sEKLQahaEKLLAAGKRMLSF-------GGDH---FVTLPLLRAHAKHFGKMALVHFDAHTDTYANG-CEFDHGTMFYTA 170
Cdd:PRK13775 106 -EQLQ---NSLSKAIKRMCDLnlkpivlGGGHetaYGHYLGLRQSLSPSDDLAVINMDAHFDLRPYDqTGPNSGTGFRQM 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130838  171 PKEGLIDP---NHSVqIGIRTE------FD---KDNG---FTVLDACQVNDRSVDDVIAQVkqIVGDMPVYLTFDIDCLD 235
Cdd:PRK13775 182 FDDAVADKrlfKYFV-LGIQEHnnnlflFDfvaKSKGiqfLTGQDIYQMGHQKVCRAIDRF--LEGQERVYLTIDMDCFS 258
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 16130838  236 PAFAPGTGTPVIGGLTSDRAIKLVRGLK-DLNIVGMDVVEVAPAYD 280
Cdd:PRK13775 259 VGAAPGVSAIQSLGVDPNLAVLVLQHIAaSGKLVGFDVVEVSPPHD 304
 
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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