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Conserved domains on  [gi|1005261216|ref|NP_001307944|]
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glycine amidinotransferase, mitochondrial isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
amidinotransferase_AGAT-like cd21136
L-arginine:glycine amidinotransferase and similar proteins; This subfamily includes eukaryotic ...
1-286 0e+00

L-arginine:glycine amidinotransferase and similar proteins; This subfamily includes eukaryotic L-arginine:glycine amidinotransferase (EC 2.1.4.1; also called glycine amidinotransferase or arginine-glycine amidinotransferase or arginine-glycine transamidinase or AT or AGAT) involved in creatine biosynthesis. L-arginine:glycine amidinotransferase (AGAT) catalyzes the committed step in creatine biosynthesis by formation of guanidinoacetic acid, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues, and may play a role in embryonic and central nervous system development and may be involved in the response to heart failure by elevating local creatine synthesis. This subfamily also contains bacterial proteins that include the virulence-associated protein HsvA from the fire blight pathogen Erwinia amylovora shown to be a polyamine amidinotransferase, and cyanobacterial SxtG, an amidinotransferase involved in the biosynthesis of paralytic shellfish toxins. The active sites of these enzymes are located in the core of the proteins at the base of a long, narrow substrate access channel. HsvA has a novel acceptor substrate specificity, with a clear preference for linear polyamines, especially putrescine and spermidine, as the amidino acceptor substrate. SxtG has a broad substrate promiscuity, operating on a wide variety of substrates and preferring alpha-amino ketones and alpha-amino methyl esters over alpha-amino acids.


:

Pssm-ID: 439148  Cd Length: 352  Bit Score: 594.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216   1 MCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGLYSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRGAK 80
Cdd:cd21136    66 LCNILEGEGVTVRRPDPVDWSQPYKTPDFESTGMYAAMPRDILLVVGNEIIEAPMAWRSRYFEYRAYRPLLKDYFKRGAK 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216  81 WTTAPKPTMADELYNQDYPIHSVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLAPDY 160
Cdd:cd21136   146 WTAAPKPTMSDELYDQDYPIESVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNRSGIEWLRRHLGPDY 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216 161 RVHIISFKDPNPMHIDATFNIIGPGIVLSNPDRPCH-QIDLFKKAGWTIITPPTPIIPDDHPLWMSSKWLSMNVLMLDEK 239
Cdd:cd21136   226 RVHILSFKDPNPMHIDATFVPLAPGLVLVNPDRPCHeQPDLFKKAGWEIVTAPTPVIPDDHPLWMSSKWLSMNVLMLDEK 305
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1005261216 240 RVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVRRR 286
Cdd:cd21136   306 RVIVEANEEPLQKMFEKLGIKPIPVPFRHANSFGGSFHCWTLDVRRR 352
 
Name Accession Description Interval E-value
amidinotransferase_AGAT-like cd21136
L-arginine:glycine amidinotransferase and similar proteins; This subfamily includes eukaryotic ...
1-286 0e+00

L-arginine:glycine amidinotransferase and similar proteins; This subfamily includes eukaryotic L-arginine:glycine amidinotransferase (EC 2.1.4.1; also called glycine amidinotransferase or arginine-glycine amidinotransferase or arginine-glycine transamidinase or AT or AGAT) involved in creatine biosynthesis. L-arginine:glycine amidinotransferase (AGAT) catalyzes the committed step in creatine biosynthesis by formation of guanidinoacetic acid, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues, and may play a role in embryonic and central nervous system development and may be involved in the response to heart failure by elevating local creatine synthesis. This subfamily also contains bacterial proteins that include the virulence-associated protein HsvA from the fire blight pathogen Erwinia amylovora shown to be a polyamine amidinotransferase, and cyanobacterial SxtG, an amidinotransferase involved in the biosynthesis of paralytic shellfish toxins. The active sites of these enzymes are located in the core of the proteins at the base of a long, narrow substrate access channel. HsvA has a novel acceptor substrate specificity, with a clear preference for linear polyamines, especially putrescine and spermidine, as the amidino acceptor substrate. SxtG has a broad substrate promiscuity, operating on a wide variety of substrates and preferring alpha-amino ketones and alpha-amino methyl esters over alpha-amino acids.


Pssm-ID: 439148  Cd Length: 352  Bit Score: 594.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216   1 MCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGLYSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRGAK 80
Cdd:cd21136    66 LCNILEGEGVTVRRPDPVDWSQPYKTPDFESTGMYAAMPRDILLVVGNEIIEAPMAWRSRYFEYRAYRPLLKDYFKRGAK 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216  81 WTTAPKPTMADELYNQDYPIHSVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLAPDY 160
Cdd:cd21136   146 WTAAPKPTMSDELYDQDYPIESVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNRSGIEWLRRHLGPDY 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216 161 RVHIISFKDPNPMHIDATFNIIGPGIVLSNPDRPCH-QIDLFKKAGWTIITPPTPIIPDDHPLWMSSKWLSMNVLMLDEK 239
Cdd:cd21136   226 RVHILSFKDPNPMHIDATFVPLAPGLVLVNPDRPCHeQPDLFKKAGWEIVTAPTPVIPDDHPLWMSSKWLSMNVLMLDEK 305
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1005261216 240 RVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVRRR 286
Cdd:cd21136   306 RVIVEANEEPLQKMFEKLGIKPIPVPFRHANSFGGSFHCWTLDVRRR 352
DdaH COG1834
N-Dimethylarginine dimethylaminohydrolase [Amino acid transport and metabolism];
4-283 2.22e-56

N-Dimethylarginine dimethylaminohydrolase [Amino acid transport and metabolism];


Pssm-ID: 441439 [Multi-domain]  Cd Length: 264  Bit Score: 182.68  E-value: 2.22e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216   4 ILKTEGVTVRRPDPIDwslkyktpdfesTGLYSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYfhrgakwtt 83
Cdd:COG1834    45 ALEALGVEVHRLPPVP------------GLPDMVFTRDAGLVIGDGAILARMRHPERRGEEAAYREWLEEL--------- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216  84 apkptmadelynqDYPIHSVEDrhklaaqgkfvttefEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLapDYRVH 163
Cdd:COG1834   104 -------------GIPVVRLPE---------------PGVFEGGDVLLDGDTLLVGYGFRTNRAGIEWLARLL--GYEVV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216 164 IISFKDPNPMHIDATFNIIGPGIVLSNPDR-PCHQIDLFKKAGWtiitpptpiipddHPLWMS---SKWLSMNVLMLDEK 239
Cdd:COG1834   154 PLELVDPRFLHLDTAFCPLAPGLALVYPEAfDPESLALLKEPGW-------------DLIEVPeeeAAWLGCNVLSLGGR 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1005261216 240 RVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDV 283
Cdd:COG1834   221 RVVSPAGNPRLNAALRAAGFEVIEVDLSEFLKGGGGFHCLTLPL 264
 
Name Accession Description Interval E-value
amidinotransferase_AGAT-like cd21136
L-arginine:glycine amidinotransferase and similar proteins; This subfamily includes eukaryotic ...
1-286 0e+00

L-arginine:glycine amidinotransferase and similar proteins; This subfamily includes eukaryotic L-arginine:glycine amidinotransferase (EC 2.1.4.1; also called glycine amidinotransferase or arginine-glycine amidinotransferase or arginine-glycine transamidinase or AT or AGAT) involved in creatine biosynthesis. L-arginine:glycine amidinotransferase (AGAT) catalyzes the committed step in creatine biosynthesis by formation of guanidinoacetic acid, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues, and may play a role in embryonic and central nervous system development and may be involved in the response to heart failure by elevating local creatine synthesis. This subfamily also contains bacterial proteins that include the virulence-associated protein HsvA from the fire blight pathogen Erwinia amylovora shown to be a polyamine amidinotransferase, and cyanobacterial SxtG, an amidinotransferase involved in the biosynthesis of paralytic shellfish toxins. The active sites of these enzymes are located in the core of the proteins at the base of a long, narrow substrate access channel. HsvA has a novel acceptor substrate specificity, with a clear preference for linear polyamines, especially putrescine and spermidine, as the amidino acceptor substrate. SxtG has a broad substrate promiscuity, operating on a wide variety of substrates and preferring alpha-amino ketones and alpha-amino methyl esters over alpha-amino acids.


Pssm-ID: 439148  Cd Length: 352  Bit Score: 594.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216   1 MCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGLYSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRGAK 80
Cdd:cd21136    66 LCNILEGEGVTVRRPDPVDWSQPYKTPDFESTGMYAAMPRDILLVVGNEIIEAPMAWRSRYFEYRAYRPLLKDYFKRGAK 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216  81 WTTAPKPTMADELYNQDYPIHSVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLAPDY 160
Cdd:cd21136   146 WTAAPKPTMSDELYDQDYPIESVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNRSGIEWLRRHLGPDY 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216 161 RVHIISFKDPNPMHIDATFNIIGPGIVLSNPDRPCH-QIDLFKKAGWTIITPPTPIIPDDHPLWMSSKWLSMNVLMLDEK 239
Cdd:cd21136   226 RVHILSFKDPNPMHIDATFVPLAPGLVLVNPDRPCHeQPDLFKKAGWEIVTAPTPVIPDDHPLWMSSKWLSMNVLMLDEK 305
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1005261216 240 RVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVRRR 286
Cdd:cd21136   306 RVIVEANEEPLQKMFEKLGIKPIPVPFRHANSFGGSFHCWTLDVRRR 352
amidinotransferase-like cd21113
L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar ...
1-286 2.77e-133

L-arginine:glycine amidinotransferase, inosamine-phosphate amidinotransferase and similar proteins; This family contains amidinotransferase enzymes known to catalyze the transfer of the amidino group from a donor molecule (usually arginine) to an acceptor molecule bearing a primary amine. They are widespread in nature, occurring in essential metabolic pathways in eukaryotes as well as in biosynthetic pathways for antibiotics and virulence factors in prokaryotes. This family includes L-arginine:glycine amidinotransferase (EC 2.1.4.1; also called glycine amidinotransferase, arginine-glycine amidinotransferase, or arginine-glycine transamidinase), inosamine-phosphate amidinotransferase (EC 2.1.4.2; also called inosamine amidinotransferase, inosamine-P amidinotransferase, or scyllo-inosamine-4-phosphate amidinotransferase or L-arginine:inosamine phosphate amidinotransferase), and similar proteins. L-arginine:glycine amidinotransferase (AT or AGAT) catalyzes the committed step in creatine biosynthesis by formation of guanidinoacetic acid, the immediate precursor of creatine. Inosamine-phosphate amidinotransferases catalyze two nonconsecutive transamidination reactions in the biosynthesis of the streptomycin family of antibiotics. This family also includes L-arginine:inosamine-phosphate Streptomyces griseus amidinotransferase StrB1, which is structurally similar to human L-arginine:glycine amidinotransferase; AT and StrB1 share conserved residues involved in substrate binding and catalysis at equivalent topological positions, suggesting a similar reaction mechanism among amidinotransferases.


Pssm-ID: 439146  Cd Length: 336  Bit Score: 381.08  E-value: 2.77e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216   1 MCNILKTEGVTVRRPDPIDWsLKYKTPDFESTGLysaMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRG-A 79
Cdd:cd21113    65 LASILEKEGVRVRRPKEVDH-LPAKTPDGETTGV---MPRDILFVIGNKIIEAPMAWPSRFFEELAYRDILEDYGESGlY 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216  80 KWTTAPKPTMADELYNQdypihsvedrhkLAAQGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLAPD 159
Cdd:cd21113   141 RVMRAPKPEGGDDLYDG------------QAPAGEDIITETEPLFDAADFMRFGKDIIGQRSQVTNMKGIEWLREYLGDD 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216 160 YRVHIISFKDPNPMHIDATFNIIGPGIVLSNPDRPCH--QIDLFKKaGWTIITPPTPIIPDDHPLWMSSKWLSMNVLMLD 237
Cdd:cd21113   209 YTVHIIELDDPHPMHLDCTFLPLREGLALIYPSRVVEprQIPDFFK-GWELINVPEYPEPDDHPLYMCSNWLGTNVLSLD 287
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1005261216 238 EKRVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVRRR 286
Cdd:cd21113   288 EKTIIVERREVHLNRQLRKLGMNVIEIPFYHAISLGGGFHCATMDLVRE 336
amidinotransferase_StrB1-like cd21135
L-arginine:inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus (StrB1) and ...
1-292 1.88e-84

L-arginine:inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus (StrB1) and similar proteins; This subfamily includes inosamine-phosphate amidinotransferase (EC 2.1.4.2; also called inosamine amidinotransferase or inosamine-P amidinotransferase or scyllo-inosamine-4-phosphate amidinotransferase or L-arginine:inosamine phosphate amidinotransferase) from Streptomyces griseus (StrB1), among others. Inosamine-phosphate amidinotransferase catalyzes two non-consecutive transamidination reactions; it converts scyllo-inosamine 4-phosphate into N-amidino-scyllo-inosamine 4-phosphate, and N1-amidinostreptamine 6-phosphate into streptidine 6-phosphate. L-arginine:inosamine-phosphate amidinotransferase StrB1 is structurally similar to the human L-arginine:glycine amidinotransferase (AT), with residues involved in substrate binding and catalysis conserved in AT and StrB1 at equivalent topological positions, suggesting a similar reaction mechanism among amidinotransferases. This subfamily also includes putative inosamine-phosphate amidinotransferase 2 (StrB2), also called aminocyclitol amidinotransferase or inosamine-phosphate amidinotransferase II, from Streptomyces glaucescens. It is unclear if StrB2 participates in streptomycin biosynthesis as it contains an arginine residue instead of the nucleophilic cysteine that is a key residue for amidine transfer.


Pssm-ID: 439147  Cd Length: 343  Bit Score: 256.97  E-value: 1.88e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216   1 MCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGLYSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRGAK 80
Cdd:cd21135    65 LCEELTKLGVTVRRPGPRDHAAPFKTPDWETDGFYDYCPRDGLLPVGQTIIETPMALRSRFLESFAYKDLLLEYFASGSR 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216  81 WTTAPKPTMADELYNQDYPIHSvedrhklaaqgkfVTTEFEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLAPDY 160
Cdd:cd21135   145 WISAPKPRLTDDMYDPTAPAGE-------------RLRDLEPVFDAANVLRIGTDLLYLVSDSGNELGARWLQSALGDRY 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216 161 RVHIISFKDPNPmHIDATFNIIGPGIVLSNPDR--PCHQIDLFKKagWTIIT---PPTPIIPDDHPLwmSSKWLSMNVLM 235
Cdd:cd21135   212 TVHPCRGLYAST-HIDSTIVPLRPGLVLVNPERvnDDNLPPFLRS--WDRIWcpeLVDIGYTGDKPH--CSAWIGMNLLV 286
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1005261216 236 LDEKRVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVRRRGTLQSY 292
Cdd:cd21135   287 VRPGLAVVDRRQTPLIRVLEKHGIDVLPLQLTHARTLGGGFHCVTLDVRRTGTLETY 343
DdaH COG1834
N-Dimethylarginine dimethylaminohydrolase [Amino acid transport and metabolism];
4-283 2.22e-56

N-Dimethylarginine dimethylaminohydrolase [Amino acid transport and metabolism];


Pssm-ID: 441439 [Multi-domain]  Cd Length: 264  Bit Score: 182.68  E-value: 2.22e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216   4 ILKTEGVTVRRPDPIDwslkyktpdfesTGLYSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYfhrgakwtt 83
Cdd:COG1834    45 ALEALGVEVHRLPPVP------------GLPDMVFTRDAGLVIGDGAILARMRHPERRGEEAAYREWLEEL--------- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216  84 apkptmadelynqDYPIHSVEDrhklaaqgkfvttefEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLapDYRVH 163
Cdd:COG1834   104 -------------GIPVVRLPE---------------PGVFEGGDVLLDGDTLLVGYGFRTNRAGIEWLARLL--GYEVV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005261216 164 IISFKDPNPMHIDATFNIIGPGIVLSNPDR-PCHQIDLFKKAGWtiitpptpiipddHPLWMS---SKWLSMNVLMLDEK 239
Cdd:COG1834   154 PLELVDPRFLHLDTAFCPLAPGLALVYPEAfDPESLALLKEPGW-------------DLIEVPeeeAAWLGCNVLSLGGR 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1005261216 240 RVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDV 283
Cdd:COG1834   221 RVVSPAGNPRLNAALRAAGFEVIEVDLSEFLKGGGGFHCLTLPL 264
 
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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