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Query: [E] COG0169 Shikimate 5-dehydrogenase, from VFDB

Results of FFAS03 search in H.sapiens
Master-slave alignment(slide right to see more) does not show gaps in the query sequence, use ali links to display alignment between query and templates.
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# Score Template Links and tools%idFirst MASQIDQYAVFGNPINHSKSPFIHTLFARQTQQSMIYTAQCVPVDGFTEAAKHFFAQGGRGCNVTVPFKEEAYRFADRLTERARLAGAVNTLKKLDDGEILGDNTDGEGLVQDLLAQQVLLKGATILLIGAGGAARGVLKPLLDQQPASITVTNRTFAKAEQLAELVAAYGEVKAQAFEQLKQSYDVIINSTSASLDGELPAIDPVIFSSRSVCYDMMYGKGYTVFNQWARQHGCAQAIDGLGMLVGQAAESFMLWRGLRPGTKQILRELRKNLEGALLast
1 -14.700sp|Q9UDR5|AASS_HUMAN Alpha-aminoadipic semialdehyde synthase, mitochondrial OS=Homo sapiens GN=AASS PE=1 SV=1  ali   16  1...............................................................................................SNGTL----PDKYKYIQTLRESRERAQSRKVLVLGSGYISEPVLEYLSRDGNIEITVGSDMKNQIEQLGKKYNINPVSQEEKLGFLVAKQDLVISLLPYVLH---PLVAKACITNKVNMVTASYITPALKELEKSVEDAGITIIGELGL.................................. 153
2 -12.500sp|Q6UB35|C1TM_HUMAN Monofunctional C1-tetrahydrofolate synthase, mitochondrial OS=Homo sapiens GN=MTHFD1L PE=1 SV=1  ali   10  104.........QAGDDNLMQEI---NQNLAEEAGLNITHICLDSSEAEIIDEILKINETRVHGLALQISENLFSNKVLNALKPEKD----VDGVTDINLGKLVRGDAHAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQW------------------KTRQLQSKLHEADIVVLGS-----PKPEEIPLTWIQPGTTVLNCSHDFLSGKV.................................................... 300
3 -12.300sp|Q9UDR5|AASS_HUMAN Alpha-aminoadipic semialdehyde synthase, mitochondrial OS=Homo sapiens GN=AASS PE=1 SV=1  ali   13  66....MTECTTIEHPF-CMYDADQHIIHDSVEGSGILMCSIDNLPAQLPIEATECFG------DMLYPYVEEMIL-ATQPLESQNFSPVVRDAVITSNGTLPDKYKYIQTLREERAQSLSMGTRRKVLVLGSGYISEPVLEYLSRDGNIEITVGSDMKNQIEQLGKKYNINPVSQEEKLGFLVAKQDLVISLLPYVLH---PLVAKACITNKVNMVTASYTPALKELEKSVEDAGITIIGE...................................... 300
4 -10.300sp|P13995|MTDC_HUMAN(removed signalp:1-20) Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial OS=Homo sapiens GN=MTHFD2 PE=1 SV=2  ali follow..  11  54.........LVGENPASHSYVLNKTRAAAVVGINSETIMKSISEEELLNLINKLNNDNVDGLLVQLPLPEHIDE--RRICNAVSPDKDVDGFHVINVGRMCLDQYTPWGVWEIIKRTGIPTLGKNVVVAGRSKVGMPIAMLLHTDGAHERPGGDATVTISHR---------YTPKEQLKKHTILADIVISAA-----GIPNLITADMIKEGAAVIDVGINRVHDPVTAKPKLVGITPVPGGVGMLMKNTIIAAKKVLRLEEREVLKSKEL........ 325
5 -10.100sp|Q9H903|MTD2L_HUMAN Probable bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2 OS=Homo sapiens GN=MTHFD2L PE=2 SV=2  ali follow..  10  30.........LVGDNPASHTYVRNKIRAASAVGICSELILKDVSQEELLDVTDQLNMPRVSGILVQLPLPDHVDE--RTICNGIAPEKDVDGFHIINIGRLCLDQHS-SAVWEIIKRTGIQTFGKNVVVAGRSKVGMPIAMLLHTDGEHERPGGDATVTIAHR---------YTPKEQLKIHTQLADIIIVAA-----GIPKLITSDMVKEGAAVIDVGINYVHDPVTGKTKLVGITPVPGGVGMLLKNTLLAAK........................ 285
6 -10.000sp|P11586|C1TC_HUMAN C-1-tetrahydrofolate synthase, cytoplasmic OS=Homo sapiens GN=MTHFD1 PE=1 SV=3  ali   11  42.........QVGNRDDSNLYINVKLKAAEEIGIKATHIKLTTTESEVMKYITSLNESTVHGFLVQLPLDSENSINTEEVINAIAPEKDVDGLTSINAGRLARGDLN-KGCLELIKETGVPIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHS------------------KTAHLDEEVNKGDILVVAT-----GQPEMVKGEWIKPGAIVIDCGINYVDVAYDEAKERASFITPVPGVAMLMQSTVESAKRFLEKFKP................ 300
7 -9.520sp|O75911|DHRS3_HUMAN(removed signalp:1-23) Short-chain dehydrogenase/reductase 3 OS=Homo sapiens GN=DHRS3 PE=1 SV=2  ali follow..  13  1............................................................................................................AVGLVLPAKLRDLSRENVLITGGGGIGRQLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGT--AKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHINTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDC. 186
8 -9.430sp|Q14894|CRYM_HUMAN Mu-crystallin homolog OS=Homo sapiens GN=CRYM PE=1 SV=1  ali follow..  15  89.................................................................VPSHQATVLLFEPSNGTLLAVMDGNVITAKRTAAVSAIATKFLK----------PPSSEVLCILGAGVQAYSHYEIFTEFSFKEVRIWNRTKENAEKFADTVQGEVRV-CSSVQEAVAGADVIITVTLAASRPDWRELDDELMKEAVLYVD.............................................................. 249
9 -9.150sp|Q6UB35|C1TM_HUMAN Monofunctional C1-tetrahydrofolate synthase, mitochondrial OS=Homo sapiens GN=MTHFD1L PE=1 SV=1  ali   11  1........................................................TRVHGLALQISENLFSNKVLNALKPEKD----VDGVTDINLGKLVRGDAHAKAVIELLEKSGVNLDGKKILVVGAHGSLEAALQCLFQRKGSMTMSIQW------------------KTRQLQSKLHEADIVVLGS-----PKPEEIPLTWIQPGTTVLNCSHDFLSGKVGSPRIHFGGLIEEDDVILRIQNMVSSGRRWLREQQHRRWRLHCLKLQPLSPV 209
10 -8.950sp|Q7Z624|CLNMT_HUMAN Calmodulin-lysine N-methyltransferase OS=Homo sapiens GN=CLNMT PE=1 SV=2  ali follow..  8  134.............................................................................................................LAYYCLKHNNIFRALAVCELGGGMTCLAGLMVAISADVKEVLLTDGNEKAIRNVQDIITRNQKAGVFKTQKISGHFDIVMCA------------------------DCLFLDQYRASL-----------VDAIKRLLQPRGKAMVFAPRRGNTLNQFCNLAEKA..... 278
FFAS is supported by the NIH grant R01-GM087218-01
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Selected papers from Godzik Lab
Ying Zhang, Ines Thiele, Dana Weekes, Zhanwen Li, Lukasz Jaroszewski, Krzysztof Ginalski, Ashley Deacon, John Wooley, Scott Lesley, Ian Wilson, Bernhard Palsson, Andrei Osterman, Adam Godzik. Three-Dimensional Structural View of the Central Metabolic Network of Thermotoga maritima. Science. 2009 Sep 18;325(5947):1544-9.

Mayya Sedova, Mallika Iyer, Zhanwen Li, Lukasz Jaroszewski, Kai W Post, Thomas Hrabe, Eduard Porta-Pardo, Adam Godzik Cancer3D 2.0:: interactive analysis of 3D patterns of cancer mutations in cancer subsets. Nucleic Acids Research, gky1098 2018; Published on November 8 2018.

Pawlowski K, Pio F, Chu Z, Reed JC, Godzik A. PAAD - a new protein domain associated with apoptosis, cancer and autoimmune diseases. Trends Biochem Sci. 2001 Feb;26(2):85-7.