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Adenylosuccinate lyase (ASL) (EC 4.3.2.2) (Adenylosuccinase) (ASase) (Glutamyl--tRNA ligase regulatory factor)

 PUR8_BACSU              Reviewed;         431 AA.
P12047;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
10-APR-2019, entry version 151.
RecName: Full=Adenylosuccinate lyase;
Short=ASL;
EC=4.3.2.2;
AltName: Full=Adenylosuccinase;
Short=ASase;
AltName: Full=Glutamyl--tRNA ligase regulatory factor;
Name=purB; Synonyms=purE; OrderedLocusNames=BSU06440;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3036807;
Ebbole D.J., Zalkin H.;
"Cloning and characterization of a 12-gene cluster from Bacillus
subtilis encoding nine enzymes for de novo purine nucleotide
synthesis.";
J. Biol. Chem. 262:8274-8287(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
PROTEIN SEQUENCE OF 1-30.
STRAIN=168 / BGSC1A1;
PubMed=1608947; DOI=10.1073/pnas.89.12.5389;
Gendron N., Breton R., Champagne N., Lapointe J.;
"Adenylosuccinate lyase of Bacillus subtilis regulates the activity of
the glutamyl-tRNA synthetase.";
Proc. Natl. Acad. Sci. U.S.A. 89:5389-5392(1992).
[4]
CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF HIS-89; HIS-141;
GLN-212; ASN-270 AND ARG-301.
PubMed=15182182; DOI=10.1021/bi0494774;
Segall M.L., Colman R.F.;
"Gln212, Asn270, and Arg301 are critical for catalysis by
adenylosuccinate lyase from Bacillus subtilis.";
Biochemistry 43:7391-7402(2004).
[5]
SUBUNIT.
PubMed=18237141; DOI=10.1021/bi701400c;
De Zoysa Ariyananda L., Colman R.F.;
"Evaluation of types of interactions in subunit association in
Bacillus subtilis adenylosuccinate lyase.";
Biochemistry 47:2923-2934(2008).
[6]
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS).
PubMed=10926519; DOI=10.1006/jmbi.2000.3970;
Toth E.A., Worby C., Dixon J.E., Goedken E.R., Marqusee S.,
Yeates T.O.;
"The crystal structure of adenylosuccinate lyase from Pyrobaculum
aerophilum reveals an intracellular protein with three disulfide
bonds.";
J. Mol. Biol. 301:433-450(2000).
-!- FUNCTION: Influences the affinity of glutamyl--tRNA ligase for its
substrates and increases its thermostability.
-!- CATALYTIC ACTIVITY:
Reaction=N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate;
Xref=Rhea:RHEA:16853, ChEBI:CHEBI:29806, ChEBI:CHEBI:57567,
ChEBI:CHEBI:456215; EC=4.3.2.2;
Evidence={ECO:0000269|PubMed:15182182};
-!- CATALYTIC ACTIVITY:
Reaction=(2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-
ribosyl)imidazole-4-carboxamide + fumarate;
Xref=Rhea:RHEA:23920, ChEBI:CHEBI:29806, ChEBI:CHEBI:58443,
ChEBI:CHEBI:58475; EC=4.3.2.2;
Evidence={ECO:0000269|PubMed:15182182};
-!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
AMP from IMP: step 2/2.
-!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-
amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
-!- SUBUNIT: Homotetramer. Residues from neighboring subunits
contribute catalytic and substrate-binding residues to each active
site. {ECO:0000269|PubMed:15182182, ECO:0000269|PubMed:18237141}.
-!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J02732; AAA22676.1; -; Genomic_DNA.
EMBL; AL009126; CAB12464.1; -; Genomic_DNA.
PIR; C29326; WZBSDS.
RefSeq; NP_388526.1; NC_000964.3.
RefSeq; WP_003233955.1; NZ_JNCM01000032.1.
PDB; 1F1O; X-ray; 3.25 A; A=1-431.
PDBsum; 1F1O; -.
ProteinModelPortal; P12047; -.
SMR; P12047; -.
IntAct; P12047; 3.
MINT; P12047; -.
STRING; 224308.BSU06440; -.
PaxDb; P12047; -.
PRIDE; P12047; -.
EnsemblBacteria; CAB12464; CAB12464; BSU06440.
GeneID; 936048; -.
KEGG; bsu:BSU06440; -.
PATRIC; fig|224308.179.peg.700; -.
eggNOG; ENOG4105C83; Bacteria.
eggNOG; COG0015; LUCA.
HOGENOM; HOG000033912; -.
InParanoid; P12047; -.
KO; K01756; -.
OMA; ASSCEKI; -.
PhylomeDB; P12047; -.
BioCyc; BSUB:BSU06440-MONOMER; -.
BRENDA; 4.3.2.2; 658.
SABIO-RK; P12047; -.
UniPathway; UPA00074; UER00132.
UniPathway; UPA00075; UER00336.
EvolutionaryTrace; P12047; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity; IBA:GO_Central.
GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IDA:MGI.
GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central.
GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006167; P:AMP biosynthetic process; IDA:MGI.
Gene3D; 1.10.275.10; -; 1.
InterPro; IPR019468; AdenyloSucc_lyase_C.
InterPro; IPR024083; Fumarase/histidase_N.
InterPro; IPR020557; Fumarate_lyase_CS.
InterPro; IPR000362; Fumarate_lyase_fam.
InterPro; IPR022761; Fumarate_lyase_N.
InterPro; IPR008948; L-Aspartase-like.
InterPro; IPR004769; Pur_lyase.
Pfam; PF10397; ADSL_C; 1.
Pfam; PF00206; Lyase_1; 1.
PRINTS; PR00149; FUMRATELYASE.
SMART; SM00998; ADSL_C; 1.
SUPFAM; SSF48557; SSF48557; 1.
TIGRFAMs; TIGR00928; purB; 1.
PROSITE; PS00163; FUMARATE_LYASES; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; Lyase;
Purine biosynthesis; Reference proteome.
CHAIN 1 431 Adenylosuccinate lyase.
/FTId=PRO_0000137873.
REGION 4 5 Substrate binding. {ECO:0000250}.
REGION 67 69 Substrate binding. {ECO:0000250}.
REGION 93 94 Substrate binding. {ECO:0000250}.
REGION 268 270 Substrate binding. {ECO:0000250}.
ACT_SITE 141 141 Proton donor/acceptor. {ECO:0000250}.
ACT_SITE 262 262 Proton donor/acceptor. {ECO:0000250}.
BINDING 212 212 Substrate. {ECO:0000250}.
BINDING 276 276 Substrate. {ECO:0000250}.
BINDING 301 301 Substrate. {ECO:0000250}.
BINDING 306 306 Substrate. {ECO:0000250}.
MUTAGEN 89 89 H->Q: Abolishes enzyme activity.
{ECO:0000269|PubMed:15182182}.
MUTAGEN 141 141 H->Q: Abolishes enzyme activity.
{ECO:0000269|PubMed:15182182}.
MUTAGEN 212 212 Q->E: Decreases catalytic activity 1000-
fold. {ECO:0000269|PubMed:15182182}.
MUTAGEN 212 212 Q->M: Abolishes enzyme activity.
{ECO:0000269|PubMed:15182182}.
MUTAGEN 270 270 N->D,L: Abolishes enzyme activity.
{ECO:0000269|PubMed:15182182}.
MUTAGEN 301 301 R->K,Q: Abolishes enzyme activity.
{ECO:0000269|PubMed:15182182}.
CONFLICT 5 5 Y -> K (in Ref. 3; AA sequence).
{ECO:0000305}.
SEQUENCE 431 AA; 49485 MW; 89D2ED7F7F6D46A2 CRC64;
MIERYSRPEM SAIWTDENRF QAWLEVEILA CEAWAELGVI PKEDVKVMRE NASFDINRIL
EIEKDTRHDV VAFTRAVSES LGEERKWVHY GLTSTDVVDT ALSYLLKQAN DILLKDLERF
VDIIKEKAKE HKYTVMMGRT HGVHAEPTTF GLKLALWHEE MKRNLERFKQ AKAGIEVGKI
SGAVGTYANI DPFVEQYVCE KLGLKAAPIS TQTLQRDRHA DYMATLALIA TSIEKFAVEI
RGLQKSETRE VEEFFAKGQK GSSAMPHKRN PIGSENMTGM ARVIRGYMMT AYENVPLWHE
RDISHSSAER IILPDATIAL NYMLNRFSNI VKNLTVFPEN MKRNMDRTLG LIYSQRVLLA
LIDTGLTREE AYDTVQPKAM EAWEKQVPFR ELVEAEEKIT SRLSPEKIAD CFDYNYHLKN
VDLIFERLGL A


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Pathways :
WP1030: Selenium metabolism Selenoproteins
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP106: Alanine and aspartate metabolism
WP108: Selenium metabolism/Selenoproteins
WP1097: Non-homologous end joining
WP1149: Selenium metabolism Selenoproteins
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1201: Non-homologous end joining
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP1208: Non-homologous end joining
WP1222: Non-homologous end joining
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP1242: Non-homologous end joining
WP1277: Non-homologous end joining
WP1293: Selenium metabolism Selenoproteins
WP1324: Non-homologous end joining
WP1358: Selenium metabolism Selenoproteins
WP1493: Carbon assimilation C4 pathway
WP1570: Non-homologous end joining
WP1620: Aminoacyl-tRNA biosynthesis
WP1625: Base excision repair
WP1640: Cysteine and methionine metabolism
WP1672: Mismatch repair
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair

Related Genes :
[ADSL AMPS] Adenylosuccinate lyase (ADSL) (ASL) (EC 4.3.2.2) (Adenylosuccinase) (ASase)
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BANRA_00208 BANRA_00433 BHF46_18455 BMT91_24760 C4J69_22715 C7B08_25495 CR538_10415 D2F89_25795 D3Y67_22910 D9G42_11130 D9H12_21840 D9I52_00260 D9J11_25195 DP258_02540 EC3234A_36c00010 EFV06_13085 NCTC8500_02249 NCTC9037_02122 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CG691_19145 CG705_13560 CG706_14580 CIJ94_05515 COD46_23180 CQP61_17160 CRD98_26150 D3I61_11545 D5653_07335 D9D20_21030 D9D23_19420 D9D43_06110 D9D77_14400 D9H68_20750 D9H70_25730 D9H84_23295 DL800_09215 DLU27_07380 DNQ41_14245 DQE83_22775 DTL43_21780 DTM25_06080 DU290_13085 DU321_04440 E2855_02503 EAI36_14435 EC95NR1_00961 ED648_25045 ED653_23400 ED658_13700 ERS085379_01273 ERS085386_05041 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[APEX1 APE APE1 APEX APX HAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (APE-1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[myrf-2 F21A10.2] Myelin regulatory factor homolog 2 (EC 3.4.-.-) [Cleaved into: Myelin regulatory factor homolog 2, N-terminal; Myelin regulatory factor homolog 2, C-terminal]
[pyrG A6592_02570 A8M42_16405 A9R57_06965 AC067_22330 AC789_1c31020 ACN002_2797 ACN77_07080 ACN81_20385 ACU57_24415 ACU90_23015 AJ318_22735 AKG99_03555 AM270_00945 AM446_06950 AM464_05605 AM465_10605 AML07_12460 AML35_05300 APT94_17890 APU18_18535 APZ14_09290 ARC77_10140 AU473_08010 AUQ13_17535 AUS26_15660 AW059_10675 AW106_00665 AWP75_20610 AZZ83_003241 B1K96_20050 B7C53_10055 B9M99_21725 B9N33_09475 B9T59_19685 BANRA_01020 BANRA_01301 BANRA_01853 BANRA_03509 BANRA_04184 BANRA_04324 BB545_13920 BE963_03670 BEN53_16995 BET08_07180 BH694_13410 BHF46_05050 BHS81_16640 BHS87_15735 BIQ87_15835 BIU72_09520 BIZ41_16885 BJJ90_05265 BK248_12970 BK292_23205 BK334_11935 BK373_15870 BK375_10085 BK383_11680 BK400_05820 BMT49_17330 BMT53_21250 BMT91_11105 BN17_26661 BTQ04_11510 BTQ06_23845 BUE81_06975 BVL39_12970 BW690_04975 BWP17_05185 BXT93_24405 BZL31_00820 BZL69_02125 C1I57_04860 C2M16_17770 C2U48_20025 C4J69_11655 C4K41_05275 C4M78_00835 C5715_23540 C5N07_06155 C5P01_05005 C5P43_15935 C5P44_09340 C6669_14670 C6986_17750 C6B13_03370 C7235_05745 C7B02_19400 C7B06_11630 C7B07_14530 C7B08_01430 C9E25_03325 CA593_12975 CCZ14_04445 CCZ17_10850 CDL37_13440 CG691_07365 CG692_07005 CG705_05530 CG706_07860 CIJ94_12220 COD30_01795 COD46_07095 CQP61_06810 CR538_05495 CR539_18815 CRE06_03485 CRM83_26360 CRT43_16405 CRT46_16440 CSB64_15850 CT143_09630 CT146_00680 CV83915_03339 CVH05_06295 CWM24_00790 CWS33_03125 CXB56_08765 D0X26_06660 D1900_12730 D2183_19100 D2F89_14380 D3821_11140 D3I61_16000 D3Y67_06430 D6X47_20010 D6Z21_06885 D7Y10_03025 D9D20_04450 D9D23_22915 D9D33_19300 D9D43_17525 D9D65_14225 D9D69_09045 D9D77_00700 D9E30_05150 D9E35_20180 D9F02_13015 D9F06_14905 D9F12_20360 D9F17_11720 D9F21_05730 D9F57_14060 D9G11_10545 D9G22_12025 D9G42_05640 D9G48_11875 D9G53_18355 D9H12_01020 D9H53_12755 D9H66_06795 D9H68_17340 D9H70_12195 D9H84_05175 D9H94_16855 D9I18_10690 D9I20_00375 D9I47_00795 D9I52_20775 D9I82_09360 D9I88_14405 D9I93_14040 D9J03_22055 D9J11_17735 D9J39_15575 D9J44_16360 D9J46_14445 D9J48_09915 D9J60_10045 D9K10_07620 D9L99_02095 DD762_13665 DIV22_29760 DL545_05995 DL800_20505 DM129_10705 DM262_13330 DMZ31_10015 DNQ41_18960 DNR41_08670 DOT75_04395 DP258_16075 DQE83_04685 DQP22_07305 DS732_20695 DS966_06010 DTL43_09355 DTL90_02675 DTM10_03745 DTM25_22630 DTM45_13530 DU284_12985 DU290_05405 DU309_08860 DU326_11595 E2855_03617 EA140_01780 EAI36_21600 EAI42_07155 EAI44_18400 EAI52_12500 EB510_16355 EB553_05185 EB569_00660 EB595_11470 EC1094V2_904 EC3234A_48c00890 EC95NR1_02021 ECONIH1_15890 ECs3640 ED060_03420 ED098_15385 ED124_16450 ED133_03895 ED287_02625 ED600_14885 ED648_01520 ED653_00705 ED944_03505 EEO96_21535 EEP03_03515 EEP23_14050 EF364_03510 EFV06_07140 EGN87_18575 EGT48_09620 EGY17_03100 EIA08_07275 EIA21_04795 EL75_0914 EL79_0915 EL80_0918 ERS085365_02427 ERS085366_03042 ERS085374_03279 ERS085386_03410 ERS085416_02898 ERS139211_02072 ERS150873_02003 ERS150876_01467 FORC28_1110 GJ11_18025 HMPREF3040_01161 HW43_18180 JD73_16335 MJ49_17095 MS6198_30910 MS8345_02965 NCTC10082_03473 NCTC10090_04050 NCTC10418_01701 NCTC10764_00296 NCTC10766_00690 NCTC10767_02309 NCTC11022_02860 NCTC11112_00121 NCTC11181_03277 NCTC12950_01251 NCTC13125_04353 NCTC13127_01436 NCTC13462_04807 NCTC13846_01212 NCTC7152_00995 NCTC7927_01209 NCTC8500_01090 NCTC8960_03783 NCTC9007_03892 NCTC9036_01135 NCTC9037_01243 NCTC9044_00576 NCTC9045_01221 NCTC9050_04166 NCTC9054_01172 NCTC9058_00847 NCTC9062_02131 NCTC9075_01630 NCTC9077_01409 NCTC9081_05851 NCTC9117_01609 NCTC9119_01271 NCTC9434_01004 NCTC9706_03296 NCTC9775_04845 NCTC9777_02704 NCTC9969_01292 PU06_02080 RG28_07675 RK56_023165 SAMEA3472033_01264 SAMEA3472044_02272 SAMEA3472047_00339 SAMEA3472056_05455 SAMEA3472067_02540 SAMEA3472070_01673 SAMEA3472080_03155 SAMEA3472090_00131 SAMEA3472108_00527 SAMEA3472110_03462 SAMEA3472112_03722 SAMEA3472114_02432 SAMEA3472147_03296 SAMEA3484427_03298 SAMEA3484429_03415 SAMEA3484433_01660 SAMEA3484434_01581 SAMEA3485101_02257 SAMEA3485113_02257 SAMEA3752372_03639 SAMEA3752557_03040 SAMEA3752559_02995 SAMEA3752620_01282 SAMEA3753064_02287 SAMEA3753097_02219 SAMEA3753164_01192 SAMEA3753290_02847 SAMEA3753300_01107 SAMEA3753397_04005 SK85_03024 SY51_15605 UC41_20365 UN91_03645 WM48_14990 WQ89_10170 WR15_06090 YDC107_1339] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[hchA A8M42_01610 AM465_15370 AZZ83_004235 B9N33_26475 BH694_24485 C1I57_21890 C7B02_06890 CCZ14_26645 CCZ17_22700 CRT43_11430 CT143_08220 D4L90_15900 D6X47_12880 D9D33_15385 D9E30_24120 D9E49_19020 D9F21_16730 D9I20_10460 D9I82_06925 D9J39_24905 D9J46_03345 DNR41_00375 DS966_16070 DU284_14760 DU327_11205 EA140_14775 EEO96_00675 EGN87_21410 ERS085406_02591 NCTC10766_03778 NCTC7928_05955 NCTC8450_02317 NCTC9007_02951 NCTC9075_02834 NCTC9775_01269 SY51_11150 WM48_10115] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[] Endonuclease V (EC 3.2.2.17) (DNA-(apurinic or apyrimidinic site) lyase) (AP lyase) (EC 4.2.99.18) (T4 pyrimidine dimer glycosylase) (T4-Pdg)
[nth-1 R10E4.5] Endonuclease III homolog (CeNTH) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)
[Apex1 Ape Apex Ref1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[Apex1 Ape Apex Ref1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[EPRS GLNS PARS QARS QPRS PIG32] Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) (Cell proliferation-inducing gene 32 protein) (Glutamatyl-prolyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase)]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[APEX1 APE APEX BAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[XRCC6 G22P1] X-ray repair cross-complementing protein 6 (EC 3.6.4.-) (EC 4.2.99.-) (5'-deoxyribose-5-phosphate lyase Ku70) (5'-dRP lyase Ku70) (70 kDa subunit of Ku antigen) (ATP-dependent DNA helicase 2 subunit 1) (ATP-dependent DNA helicase II 70 kDa subunit) (CTC box-binding factor 75 kDa subunit) (CTC75) (CTCBF) (DNA repair protein XRCC6) (Lupus Ku autoantigen protein p70) (Ku70) (Thyroid-lupus autoantigen) (TLAA) (X-ray repair complementing defective repair in Chinese hamster cells 6)
[Traf2] TNF receptor-associated factor 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRAF2) (RING-type E3 ubiquitin transferase TRAF2)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[mcl1 RHOS4_03500 RSP_1771] L-malyl-CoA/beta-methylmalyl-CoA lyase (EC 4.1.3.24) ((3S)-malyl-CoA/beta-methylmalyl-CoA lyase) ((S)-citramalyl-CoA lyase) (EC 4.1.3.25)
[NTHL1 NTH1 OCTS3] Endonuclease III-like protein 1 (hNTH1) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)
[ufd-2 T05H10.5] Ubiquitin conjugation factor E4 ufd-2 (EC 2.3.2.27) (E4 ubiquitin-protein ligase ufd-2) (RING-type E3 ubiquitin transferase E4) (Ubiquitin fusion degradation protein 2)

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