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Conserved domains on  [gi|500857167|ref|WP_012008671|]
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MULTISPECIES: Hsp33 family molecular chaperone HslO [Bacillus]

Protein Classification

Hsp33 family molecular chaperone HslO( domain architecture ID 11478100)

Hsp33 family molecular chaperone HslO is redox regulated and protects both thermally-unfolding and oxidatively-damaged proteins from irreversible aggregation

Gene Symbol:  hslO
Gene Ontology:  GO:0006457|GO:0051082
PubMed:  10025400|10359689
SCOP:  4003643

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
hslO PRK00114
Hsp33 family molecular chaperone HslO;
1-279 3.42e-161

Hsp33 family molecular chaperone HslO;


:

Pssm-ID: 234643  Cd Length: 293  Bit Score: 450.00  E-value: 3.42e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167   1 MDYLVKALAYDGKVRAYAANTTDTINEAQRRHHTWPTASAAIGRTMTATVMMGAMLKGENKLTVKIEGGGPIGAIIADGN 80
Cdd:PRK00114   2 ADYLVRALAEDGAVRGEAVDTTETVQEAQERHDYPPTATAALGRTLTATSLLTATLKFDGDITVQIQGDGPLGLIVVDAN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167  81 AKGQVRGYVSNPQVHFDLNEHGKLDVRRAVGTsGTLSVVKDIGLKDHFTGQTEIVSGEIGDDFTYYLVSSEQVPSSVGVG 160
Cdd:PRK00114  82 ADGQVRGYVRNPGVDLELNADGKLDVGQAVGN-GYLVVTKDPGLGEPYQGVVPLVSGEIGEDLAYYFARSEQTPSAVGLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167 161 VLVNPDNSILAAGGFIIQLLPG--TEDAVIERLEKRLSTIEPISKLIEKGMTPEEILEEVLG-EKPQILETVPVEFSCNC 237
Cdd:PRK00114 161 VLVNEDDSIKAAGGFLLQVLPGaaEDFEHLATLEERIKEEELFSLLLESGLTAEELLYRLYHeEDVKILEPQPVEFKCDC 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 500857167 238 SKERFANGIISLGKAEIDDMIEQDGQAEAQCHFCNETYVFTK 279
Cdd:PRK00114 241 SRERSANALKSLGKEELQEMIAEDGGAEMVCQFCGNKYLFDE 282
 
Name Accession Description Interval E-value
hslO PRK00114
Hsp33 family molecular chaperone HslO;
1-279 3.42e-161

Hsp33 family molecular chaperone HslO;


Pssm-ID: 234643  Cd Length: 293  Bit Score: 450.00  E-value: 3.42e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167   1 MDYLVKALAYDGKVRAYAANTTDTINEAQRRHHTWPTASAAIGRTMTATVMMGAMLKGENKLTVKIEGGGPIGAIIADGN 80
Cdd:PRK00114   2 ADYLVRALAEDGAVRGEAVDTTETVQEAQERHDYPPTATAALGRTLTATSLLTATLKFDGDITVQIQGDGPLGLIVVDAN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167  81 AKGQVRGYVSNPQVHFDLNEHGKLDVRRAVGTsGTLSVVKDIGLKDHFTGQTEIVSGEIGDDFTYYLVSSEQVPSSVGVG 160
Cdd:PRK00114  82 ADGQVRGYVRNPGVDLELNADGKLDVGQAVGN-GYLVVTKDPGLGEPYQGVVPLVSGEIGEDLAYYFARSEQTPSAVGLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167 161 VLVNPDNSILAAGGFIIQLLPG--TEDAVIERLEKRLSTIEPISKLIEKGMTPEEILEEVLG-EKPQILETVPVEFSCNC 237
Cdd:PRK00114 161 VLVNEDDSIKAAGGFLLQVLPGaaEDFEHLATLEERIKEEELFSLLLESGLTAEELLYRLYHeEDVKILEPQPVEFKCDC 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 500857167 238 SKERFANGIISLGKAEIDDMIEQDGQAEAQCHFCNETYVFTK 279
Cdd:PRK00114 241 SRERSANALKSLGKEELQEMIAEDGGAEMVCQFCGNKYLFDE 282
Hsp33 cd00498
Heat shock protein 33 (Hsp33): Cytosolic protein that acts as a molecular chaperone under ...
4-278 2.58e-141

Heat shock protein 33 (Hsp33): Cytosolic protein that acts as a molecular chaperone under oxidative conditions. In normal (reducing) cytosolic conditions, four conserved Cys residues are coordinated by a Zn ion. Under oxidative stress (such as heat shock), the Cys are reversibly oxidized to disulfide bonds, which causes the chaperone activity to be turned on. Hsp33 is homodimeric in its functional form.


Pssm-ID: 238278  Cd Length: 275  Bit Score: 398.91  E-value: 2.58e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167   4 LVKALAYDGKVRAYAANTTDTINEAQRRHHTWPTASAAIGRTMTATVMMGAMLKGENKLTVKIEGGGPIGAIIADGNAKG 83
Cdd:cd00498    1 LVRFIADDGDVRGEAVRLTETVQEALRRHDYPPTATALLGRTLVAAALLGASLKFDGRLTVQIQGDGPVGLIVADADADG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167  84 QVRGYVSNPQVHFDLNEHGKLDVRRAVGtSGTLSVVKDIGLKDHFTGQTEIVSGEIGDDFTYYLVSSEQVPSSVGVGVLV 163
Cdd:cd00498   81 TVRGYVRNPEVDLPLNEDGKLDVGDAVG-NGYLAVTKDLGLGEPYQGVVPLVSGEIAEDLEYYFAQSEQLPSAVGLGVLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167 164 NPDNSILAAGGFIIQLLPGTEDAVIERLEKRLSTIEPISKLIEKGMTPEEILEEVLGEK-PQILETVPVEFSCNCSKERF 242
Cdd:cd00498  160 NPDGTVKAAGGLLLQVLPGADEEDIDAWEKVIKLMPTVSALELLGLSPEELLYRLFHEEeVRILEKQPVRFRCDCSRERV 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 500857167 243 ANGIISLGKAEIDDMIEQDGQAEAQCHFCNETYVFT 278
Cdd:cd00498  240 AAALLTLGKEELADMIEEDGGIEVTCEFCGEKYHFD 275
HslO COG1281
Redox-regulated molecular chaperone, HSP33 family [Posttranslational modification, protein ...
1-279 1.53e-140

Redox-regulated molecular chaperone, HSP33 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440892  Cd Length: 291  Bit Score: 397.60  E-value: 1.53e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167   1 MDYLVKALAYDGKVRAYAANTTDTINEAQRRHHTWPTASAAIGRTMTATVMMGAMLKGENKLTVKIEGGGPIGAIIADGN 80
Cdd:COG1281    1 DDYLVRFLFEDGDVRGEAVRLTETVQEALARHDYPPPVTALLGEALAAAALLGATLKFDGRLTLQIQGDGPLGLLVADAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167  81 AKGQVRGYVSNPQVHFDLNEHGKLDVRRAVGtSGTLSVVKDIGLKDHFTGQTEIVSGEIGDDFTYYLVSSEQVPSSVGVG 160
Cdd:COG1281   81 SDGEVRGYARNPEVELPLNEKGKLDVGELVG-NGYLAVTIDPGLGEPYQGIVPLVGGELAEDLEYYFAQSEQLPTRVWLG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167 161 VLVNPDNsiLAAGGFIIQLLPGTEDAVIERLE--KRLSTIE---PISKLIEKGMTPEEILEEVLGE-KPQILETVPVEFS 234
Cdd:COG1281  160 VLVDEDG--WRAGGLLLQLLPGADEEAIDDEDawERAVALAatlTISELLDPGLTPEELLYRLFHEeDVRVFEPQPVRFR 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 500857167 235 CNCSKERFANGIISLGKAEIDDMIEQDGQAEAQCHFCNETYVFTK 279
Cdd:COG1281  238 CSCSRERVENALKSLGREELEDMLEEDGGIEVTCEFCNEKYRFDP 282
HSP33 pfam01430
Hsp33 protein; Hsp33 is a molecular chaperone, distinguished from all other known chaperones ...
8-278 2.12e-139

Hsp33 protein; Hsp33 is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidising conditions like H2O2 cause disulfide bonds to form in Hsp33, a process that leads to the activation of its chaperone function.


Pssm-ID: 460209  Cd Length: 271  Bit Score: 393.81  E-value: 2.12e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167    8 LAYDGKVRAYAANTTDTINEAQRRHHTWPTASAAIGRTMTATVMMGAMLKGEN-KLTVKIEGGGPIGAIIADGNAKGQVR 86
Cdd:pfam01430   1 LAEDGNVRGFAVRLTELVEEALARHDYPPVATAALGRALAAAALLGATLKFEDgRLTLQIQGDGPLGLLVADADSDGNVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167   87 GYVSNPQVHFDLNEHGkLDVRRAVGTsGTLSVVKDIGLKDHFTGQTEIVSGEIGDDFTYYLVSSEQVPSSVGVGVLVNPD 166
Cdd:pfam01430  81 GYVRNPAVELPLNEKG-LDVGGAVGD-GYLAVTKDLGLKEPYQGIVPLVSGEIAEDLTYYFAQSEQIPSAVGLGVLVDKD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167  167 NSILAAGGFIIQLLPGTEDAVIERLEKRLSTIEPISKLIEKGMTPEEILEEVL-GEKPQILETVPVEFSCNCSKERFANG 245
Cdd:pfam01430 159 GSVKAAGGLLLQLLPGADEETIDDLEERLKALPTVTDEELLELPAEELLERLFhEEDVRILEPQPVRFKCRCSRERVENA 238
                         250       260       270
                  ....*....|....*....|....*....|...
gi 500857167  246 IISLGKAEIDDMIEQDGQAEAQCHFCNETYVFT 278
Cdd:pfam01430 239 LISLGKEELEEIIEEDGKIEVTCHFCNKKYRFD 271
 
Name Accession Description Interval E-value
hslO PRK00114
Hsp33 family molecular chaperone HslO;
1-279 3.42e-161

Hsp33 family molecular chaperone HslO;


Pssm-ID: 234643  Cd Length: 293  Bit Score: 450.00  E-value: 3.42e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167   1 MDYLVKALAYDGKVRAYAANTTDTINEAQRRHHTWPTASAAIGRTMTATVMMGAMLKGENKLTVKIEGGGPIGAIIADGN 80
Cdd:PRK00114   2 ADYLVRALAEDGAVRGEAVDTTETVQEAQERHDYPPTATAALGRTLTATSLLTATLKFDGDITVQIQGDGPLGLIVVDAN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167  81 AKGQVRGYVSNPQVHFDLNEHGKLDVRRAVGTsGTLSVVKDIGLKDHFTGQTEIVSGEIGDDFTYYLVSSEQVPSSVGVG 160
Cdd:PRK00114  82 ADGQVRGYVRNPGVDLELNADGKLDVGQAVGN-GYLVVTKDPGLGEPYQGVVPLVSGEIGEDLAYYFARSEQTPSAVGLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167 161 VLVNPDNSILAAGGFIIQLLPG--TEDAVIERLEKRLSTIEPISKLIEKGMTPEEILEEVLG-EKPQILETVPVEFSCNC 237
Cdd:PRK00114 161 VLVNEDDSIKAAGGFLLQVLPGaaEDFEHLATLEERIKEEELFSLLLESGLTAEELLYRLYHeEDVKILEPQPVEFKCDC 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 500857167 238 SKERFANGIISLGKAEIDDMIEQDGQAEAQCHFCNETYVFTK 279
Cdd:PRK00114 241 SRERSANALKSLGKEELQEMIAEDGGAEMVCQFCGNKYLFDE 282
Hsp33 cd00498
Heat shock protein 33 (Hsp33): Cytosolic protein that acts as a molecular chaperone under ...
4-278 2.58e-141

Heat shock protein 33 (Hsp33): Cytosolic protein that acts as a molecular chaperone under oxidative conditions. In normal (reducing) cytosolic conditions, four conserved Cys residues are coordinated by a Zn ion. Under oxidative stress (such as heat shock), the Cys are reversibly oxidized to disulfide bonds, which causes the chaperone activity to be turned on. Hsp33 is homodimeric in its functional form.


Pssm-ID: 238278  Cd Length: 275  Bit Score: 398.91  E-value: 2.58e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167   4 LVKALAYDGKVRAYAANTTDTINEAQRRHHTWPTASAAIGRTMTATVMMGAMLKGENKLTVKIEGGGPIGAIIADGNAKG 83
Cdd:cd00498    1 LVRFIADDGDVRGEAVRLTETVQEALRRHDYPPTATALLGRTLVAAALLGASLKFDGRLTVQIQGDGPVGLIVADADADG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167  84 QVRGYVSNPQVHFDLNEHGKLDVRRAVGtSGTLSVVKDIGLKDHFTGQTEIVSGEIGDDFTYYLVSSEQVPSSVGVGVLV 163
Cdd:cd00498   81 TVRGYVRNPEVDLPLNEDGKLDVGDAVG-NGYLAVTKDLGLGEPYQGVVPLVSGEIAEDLEYYFAQSEQLPSAVGLGVLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167 164 NPDNSILAAGGFIIQLLPGTEDAVIERLEKRLSTIEPISKLIEKGMTPEEILEEVLGEK-PQILETVPVEFSCNCSKERF 242
Cdd:cd00498  160 NPDGTVKAAGGLLLQVLPGADEEDIDAWEKVIKLMPTVSALELLGLSPEELLYRLFHEEeVRILEKQPVRFRCDCSRERV 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 500857167 243 ANGIISLGKAEIDDMIEQDGQAEAQCHFCNETYVFT 278
Cdd:cd00498  240 AAALLTLGKEELADMIEEDGGIEVTCEFCGEKYHFD 275
HslO COG1281
Redox-regulated molecular chaperone, HSP33 family [Posttranslational modification, protein ...
1-279 1.53e-140

Redox-regulated molecular chaperone, HSP33 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440892  Cd Length: 291  Bit Score: 397.60  E-value: 1.53e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167   1 MDYLVKALAYDGKVRAYAANTTDTINEAQRRHHTWPTASAAIGRTMTATVMMGAMLKGENKLTVKIEGGGPIGAIIADGN 80
Cdd:COG1281    1 DDYLVRFLFEDGDVRGEAVRLTETVQEALARHDYPPPVTALLGEALAAAALLGATLKFDGRLTLQIQGDGPLGLLVADAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167  81 AKGQVRGYVSNPQVHFDLNEHGKLDVRRAVGtSGTLSVVKDIGLKDHFTGQTEIVSGEIGDDFTYYLVSSEQVPSSVGVG 160
Cdd:COG1281   81 SDGEVRGYARNPEVELPLNEKGKLDVGELVG-NGYLAVTIDPGLGEPYQGIVPLVGGELAEDLEYYFAQSEQLPTRVWLG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167 161 VLVNPDNsiLAAGGFIIQLLPGTEDAVIERLE--KRLSTIE---PISKLIEKGMTPEEILEEVLGE-KPQILETVPVEFS 234
Cdd:COG1281  160 VLVDEDG--WRAGGLLLQLLPGADEEAIDDEDawERAVALAatlTISELLDPGLTPEELLYRLFHEeDVRVFEPQPVRFR 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 500857167 235 CNCSKERFANGIISLGKAEIDDMIEQDGQAEAQCHFCNETYVFTK 279
Cdd:COG1281  238 CSCSRERVENALKSLGREELEDMLEEDGGIEVTCEFCNEKYRFDP 282
HSP33 pfam01430
Hsp33 protein; Hsp33 is a molecular chaperone, distinguished from all other known chaperones ...
8-278 2.12e-139

Hsp33 protein; Hsp33 is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidising conditions like H2O2 cause disulfide bonds to form in Hsp33, a process that leads to the activation of its chaperone function.


Pssm-ID: 460209  Cd Length: 271  Bit Score: 393.81  E-value: 2.12e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167    8 LAYDGKVRAYAANTTDTINEAQRRHHTWPTASAAIGRTMTATVMMGAMLKGEN-KLTVKIEGGGPIGAIIADGNAKGQVR 86
Cdd:pfam01430   1 LAEDGNVRGFAVRLTELVEEALARHDYPPVATAALGRALAAAALLGATLKFEDgRLTLQIQGDGPLGLLVADADSDGNVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167   87 GYVSNPQVHFDLNEHGkLDVRRAVGTsGTLSVVKDIGLKDHFTGQTEIVSGEIGDDFTYYLVSSEQVPSSVGVGVLVNPD 166
Cdd:pfam01430  81 GYVRNPAVELPLNEKG-LDVGGAVGD-GYLAVTKDLGLKEPYQGIVPLVSGEIAEDLTYYFAQSEQIPSAVGLGVLVDKD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167  167 NSILAAGGFIIQLLPGTEDAVIERLEKRLSTIEPISKLIEKGMTPEEILEEVL-GEKPQILETVPVEFSCNCSKERFANG 245
Cdd:pfam01430 159 GSVKAAGGLLLQLLPGADEETIDDLEERLKALPTVTDEELLELPAEELLERLFhEEDVRILEPQPVRFKCRCSRERVENA 238
                         250       260       270
                  ....*....|....*....|....*....|...
gi 500857167  246 IISLGKAEIDDMIEQDGQAEAQCHFCNETYVFT 278
Cdd:pfam01430 239 LISLGKEELEEIIEEDGKIEVTCHFCNKKYRFD 271
hslO PRK01402
Hsp33-like chaperonin; Reviewed
31-278 1.10e-17

Hsp33-like chaperonin; Reviewed


Pssm-ID: 234952  Cd Length: 328  Bit Score: 81.53  E-value: 1.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167  31 RHHTWPTASA-AIGRTMTATVMMGAMLKGENKLTVKIEGGGPIGAIIADGNAKGQVRGYVSnpqvhFD---LNEHGKLDV 106
Cdd:PRK01402  45 TRHDYPEPVArLLGEAVVLTVLLGSSLKFEGRFILQTQGDGPVDMLVVDFSTPDRLRAYAR-----FDeerLAAAIAAGE 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167 107 RRAvGT---SGTLSVVKDIGLK-DHFTGQTEIVSGEIGDDFTYYLVSSEQVPSSV--GVGVLVNPDNSILA---AGGFII 177
Cdd:PRK01402 120 TSP-EAllgKGHLAMTIDQGPDmQRYQGIVALDGSTLEEAAHQYFRQSEQIPTRVrlAVAELITGGGAGKPrwrAGGLLI 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500857167 178 QLLP------------------GTEDAVIER---LEKR--LSTIEPIsKLIEKGMTPEEILEEVLGEKP-QILETVPVEF 233
Cdd:PRK01402 199 QFLPqaperarqadlhpgdapeGTEIAVPEDdawVEARslVETIEDD-ELIDPTVSSERLLYRLFHERGvRVFDPQPVIA 277
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 500857167 234 SCNCSKERFANGIISLGKAEIDDMIEqDGQAEAQCHFCNETYVFT 278
Cdd:PRK01402 278 RCSCSREKIAGVLKGFSAEERADMVE-DGKISVTCEFCSRVYRFD 321
4HBD_NAD cd14860
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ...
164-216 3.00e-03

4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.


Pssm-ID: 341482  Cd Length: 371  Bit Score: 38.74  E-value: 3.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 500857167 164 NPDNSILAAGGFIIQLLPGTEDAVIERLEKRLSTIEPISKLIEKGMTPEEILE 216
Cdd:cd14860  286 NPDGEIKKLNEFLAKILGCDEEDVYDELEELLNKILPKKPLHEYGMKEEEIDE 338
 
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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