| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | g6385.t1 |
| Family | AA7 |
| Protein Properties | Length: 2402 Molecular Weight: 237189 Isoelectric Point: 5.7416 |
| Chromosome | Chromosome/Scaffold: 6 Start: 4230890 End: 4241305 |
| Description | GTP cyclohydrolase I |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 1537 | 1714 | 0 |
| RGRRPLALALPRNAEGVQACVRWALAHRRPLTVVGGGHSGHCAADGVLAVSLRHLSGVRVDAARREVTAGGGAVMGDVAAEAEAAGLAVTTGARPSVGVG LLLAGGVGHLARPHGLALDNIRAVSFVELQRGRLLRADAAALPGAFWALRGAGPCFGIVVSVTLAAHPLTTIGTLDLQ | |||
| Full Sequence |
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| Protein Sequence Length: 2402 Download |
| MGSFGGSVEA AVLEVLRALG EDPERAGLRD TPKRVAKAFK ERLVGYCQKQ WREHEFKLFE 60 EPSLQPGSPV DILDVVVHST DTSSLAPYEA RVHVSYIPLR KEVVGLSKVP RAIKLTAKQL 120 HSPASLAHAL ATRLADGLGP DRCGGVAVLV VVAAAAEGQQ QEQQQQEQLQ HVAAEEAAGQ 180 EGSAAAWLPP SPFPTLPPPP SAAARCCRVE ACVSGAYAAG LQLQPPQPPQ PQPQQPQPQQ 240 VLEMKAGAPQ WQQPAAALSR ALPACLEEFL DRAGCSNLAI SIHTTTTAID TTAPPPPPPP 300 PPPPRAAGGS GATGPTSPGP PSSSRRLPDP TSPNGPNGPT GQNDLTDPRD PTDPTDPAAD 360 PLPPPLLLAP VRRLVGAVLQ QHVPADHPAH RVVDSIARRF TADLQRATIG YSLPLLLPLV 420 PPLLPPHPNA VSASAAPPAG PTRSSSSPSC RGCCCGRSPH TLRLSFSSTC EHHMLPFSGT 480 ATLAWTCAVC GGPGGGGPGG SGRGGSDRGG SDLGGSDRGG SGPGGGSPGG GRGGCDDDGP 540 GGGGVSDYCD DGDGNGDDGC GCCVSAAAAV AAVATRALLV HSRRLSVQER ITHQLADTVG 600 AALEQLQRPP RLLRAAAVAA VAAPADADDG GGGGGDGDCD GIGDGIGGGG GGVGVLVQLR 660 ATHACMCARG TEAHGCSTTT TAAWGRGAAQ GSAARRQLCA AIRAATAAGT AGSSVSSGSS 720 SFDAFDIGGD GATARLQQQQ QSGSQGRSAL LPPPPPASPP GLPPPPPSRA WSLSLPLPAL 780 PPPPPPPPPP PPPPPPPPPP PPLPPPPAPL PPPPPPPPPP HPSPPPPPLP HLPNAIVNPI 840 HPIHSSSAHA SAAAADLAAA AAFAQLSRRS LEYGPLGAHL AALCRREAAR LGRPLAVLEL 900 GAGSGGAMRA LLRALKEEAA EEEAVPADAV AADTVAVAAA AIAGSGKAAS GTGAGARPAG 960 ASLAGANDVA SAGASVGAGA PAGLLLSRLV GRYVAVEPNA VHAAQLAEDE ELAAALLDPA 1020 AAGSSGGSGG GGGVEVVRAR LGPLPPPPAA AAGGGEKQQE REAEAVLLLP DGTPAAATAL 1080 TTACGGAPGC GGSSSGSSSG GGGGLFDLVL CCHSLYGVRP CKAAAVRWAA RQLRRGASSG 1140 GCGSGCGGGG CGCGGGGGGC VVVYHRAGEG AERLLRDLQL HQQGQEEGQE GQEEGQEGQQ 1200 QGQAGQEGPQ QGQQQGLVLE AAVQLPGGLV VTDLMGAAEG EVGEEEGQEK GEEVDSGGAA 1260 QDADMALDQL LIALGWTPPP APAPAPAAAA AATPESNTAA ATAAAADSNT AAAVDGSLGR 1320 PAAEAAAASP DEQPPQQQEK RQEQGREQGR EQQGRLLRAR FRAACVRGLP PSHPLAAALP 1380 PAAAGPCWFY DSPGVALVLR AAAGGSNTGG SSSSSSSSSR SAGHGHGNTY AASGAGAGQI 1440 PLDGPAAATA ATASTAAATL DELEAALRST VATTTTASTT ATTTATTPII TAMALDTTLG 1500 ATPSPLPPLP PPPPLLLRPG SGEYEFAMSR LKERAARGRR PLALALPRNA EGVQACVRWA 1560 LAHRRPLTVV GGGHSGHCAA DGVLAVSLRH LSGVRVDAAR REVTAGGGAV MGDVAAEAEA 1620 AGLAVTTGAR PSVGVGLLLA GGVGHLARPH GLALDNIRAV SFVELQRGRL LRADAAALPG 1680 AFWALRGAGP CFGIVVSVTL AAHPLTTIGT LDLQLPLQLP MPLPAPPLPP PPQLVPPQDL 1740 QAPPSQPPRP EAAPAPAPAA PAACGLGSEQ LAATSTGTGT GTGTGTATGT AFPPPNPAHA 1800 SAASTTKAAT TTASAASAAS SSARLLLCEY AAATAAAPRA LSADAFLYWS GPHRQRDLQL 1860 AVCTFQIPQQ RREEEQEEEK EGREEEEGRE EEEGLPVQGQ QQGPRRPQHV ELAAGDGGAG 1920 GGAGGGGGQW AASLRLAARL CAAAGVPLSE ALRRGPDAVR PTQLFDRELY MSMDARRVLT 1980 GPLQQQQQQQ QQQQQQQQQQ QQQQQQQVMG GAVESAVWGV GKEAGPAPKC GTFKRCCFLL 2040 PPPQPPAPPP PSSDDRRRRS GGDHPCGGGG GNGGDGGGGA ASCWPAGEAL LQVLAASPSP 2100 LCYVHLVHCG GAAAEPEPAA CAFGCRGWQW AAVVSGVWLL QPPPPPPQAS QPPKPPKPPP 2160 SAGATRQGSA GVAAGAAQTT AGAAAAPAVM AAAAAATAAE PAAAATAAAA EPAAAVVDPA 2220 LLAACLDGTA AVDWVYDSVR ALLPYSVGTY AADLGPSDPR DVELATHAFG GGGGGMAAAA 2280 VGAAGVKAGD GPRAPPPIGM ALDGGSDEVG CGAGADAGVE GLGWAAQVPS GAAWLGPGGG 2340 GGGGGGGGGG GRLQLLAAMK RAADPAGLLV AGAPPLLQAA ALQLAALGVG GEEAGGDGAG 2400 P* 2460 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09347 | folE | 0.0006 | 465 | 484 | 20 | + GTP cyclohydrolase I; Provisional | ||
| cd00642 | GTP_cyclohydro1 | 2.0e-20 | 7 | 141 | 135 | + GTP cyclohydrolase I (GTP-CH-I) catalyzes the conversion of GTP into dihydroneopterin triphosphate. The enzyme product is the precursor of tetrahydrofolate in eubacteria, fungi, and plants and of the folate analogs in methanogenic bacteria. In vertebrates and insects it is the biosynthtic precursor of tetrahydrobiopterin (BH4) which is involved in the formation of catacholamines, nitric oxide, and the stimulation of T lymphocytes. The biosynthetic reaction of BH4 is controlled by a regulatory protein GFRP which mediates feedback inhibition of GTP-CH-I by BH4. This inhibition is reversed by phenylalanine. The decameric GTP-CH-I forms a complex with two pentameric GFRP in the presence of phenylalanine or a combination of GTP and BH4, respectively. | ||
| PRK09347 | folE | 6.0e-22 | 9 | 118 | 110 | + GTP cyclohydrolase I; Provisional | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | XP_001224477.1 | 2e-29 | 1531 | 1718 | 270 | 475 | hypothetical protein CHGG_06821 [Chaetomium globosum CBS 148.51] |
| RefSeq | XP_001224477.1 | 0.00002 | 2090 | 2138 | 587 | 635 | hypothetical protein CHGG_06821 [Chaetomium globosum CBS 148.51] |
| RefSeq | XP_001224477.1 | 0.005 | 2227 | 2277 | 640 | 693 | hypothetical protein CHGG_06821 [Chaetomium globosum CBS 148.51] |
| RefSeq | XP_383779.1 | 5e-29 | 1498 | 1718 | 267 | 498 | hypothetical protein FG03603.1 [Gibberella zeae PH-1] |
| RefSeq | XP_383779.1 | 0.00005 | 2072 | 2138 | 590 | 667 | hypothetical protein FG03603.1 [Gibberella zeae PH-1] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2bvh_D | 4e-20 | 1539 | 1705 | 37 | 205 | A Chain A, Crystal Structure Of E.Coli Gs Mutant Dmgs(C7s;c40 |
| PDB | 2bvh_C | 4e-20 | 1539 | 1705 | 37 | 205 | A Chain A, Crystal Structure Of E.Coli Gs Mutant Dmgs(C7s;c40 |
| PDB | 2bvh_B | 4e-20 | 1539 | 1705 | 37 | 205 | A Chain A, Crystal Structure Of E.Coli Gs Mutant Dmgs(C7s;c40 |
| PDB | 2bvh_A | 4e-20 | 1539 | 1705 | 37 | 205 | A Chain A, Crystal Structure Of E.Coli Gs Mutant Dmgs(C7s;c40 |
| PDB | 2bvg_D | 4e-20 | 1539 | 1705 | 37 | 205 | A Chain A, Crystal Structure Of E.Coli Gs Mutant Dmgs(C7s;c40 |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EC180598 | 139 | 8 | 144 | 0.00000000000006 |
| EC181155 | 114 | 8 | 119 | 0.0000000000002 |
| BB903897 | 144 | 7 | 140 | 0.0000000000003 |
| HO781094 | 148 | 1 | 140 | 0.000000000001 |
| EC180515 | 114 | 8 | 119 | 0.000000000002 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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