ID B4IYX3_DROGR Unreviewed; 510 AA. AC B4IYX3; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 24-JAN-2024, entry version 77. DE SubName: Full=GH17003 {ECO:0000313|EMBL:EDV97681.1}; GN Name=Dgri\GH17003 {ECO:0000313|EMBL:EDV97681.1}; GN ORFNames=Dgri_GH17003 {ECO:0000313|EMBL:EDV97681.1}; OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Hawaiian Drosophila. OX NCBI_TaxID=7222 {ECO:0000313|Proteomes:UP000001070}; RN [1] {ECO:0000313|EMBL:EDV97681.1, ECO:0000313|Proteomes:UP000001070} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tucson 15287-2541.00 {ECO:0000313|Proteomes:UP000001070}; RX PubMed=17994087; DOI=10.1038/nature06341; RG Drosophila 12 genomes consortium; RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A., RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B., RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M., RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R., RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P., RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C., RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S., RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A., RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J., RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K., RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L., RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G., RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B., RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V., RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J., RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R., RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E., RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K., RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H., RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F., RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M., RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L., RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M., RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L., RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G., RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R., RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D., RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A., RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J., RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A., RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T., RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B., RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W., RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W., RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L., RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J., RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D., RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J., RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P., RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A., RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M., RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K., RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J., RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A., RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T., RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B., RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L., RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D., RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R., RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L., RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C., RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L., RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F., RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T., RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J., RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S., RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I., RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.; RT "Evolution of genes and genomes on the Drosophila phylogeny."; RL Nature 450:203-218(2007). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|ARBA:ARBA00001933, CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382}; CC -!- SIMILARITY: Belongs to the group II decarboxylase family. CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH916366; EDV97681.1; -; Genomic_DNA. DR RefSeq; XP_001985333.1; XM_001985297.1. DR AlphaFoldDB; B4IYX3; -. DR SMR; B4IYX3; -. DR STRING; 7222.B4IYX3; -. DR EnsemblMetazoa; FBtr0152417; FBpp0150909; FBgn0124474. DR EnsemblMetazoa; FBtr0456413; FBpp0406961; FBgn0124474. DR GeneID; 6556448; -. DR KEGG; dgr:6556448; -. DR eggNOG; KOG0629; Eukaryota. DR HOGENOM; CLU_011856_0_0_1; -. DR InParanoid; B4IYX3; -. DR OMA; RHATYHA; -. DR OrthoDB; 888358at2759; -. DR PhylomeDB; B4IYX3; -. DR Proteomes; UP000001070; Unassembled WGS sequence. DR GO; GO:0004351; F:glutamate decarboxylase activity; IEA:EnsemblMetazoa. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IEA:EnsemblMetazoa. DR GO; GO:0006538; P:glutamate catabolic process; IEA:EnsemblMetazoa. DR GO; GO:0008345; P:larval locomotory behavior; IEA:EnsemblMetazoa. DR GO; GO:0007528; P:neuromuscular junction development; IEA:EnsemblMetazoa. DR GO; GO:0008355; P:olfactory learning; IEA:EnsemblMetazoa. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:EnsemblMetazoa. DR GO; GO:0007416; P:synapse assembly; IEA:EnsemblMetazoa. DR CDD; cd06450; DOPA_deC_like; 1. DR Gene3D; 3.90.1150.170; -; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR InterPro; IPR002129; PyrdxlP-dep_de-COase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR021115; Pyridoxal-P_BS. DR PANTHER; PTHR45677:SF10; GLUTAMATE DECARBOXYLASE; 1. DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1. DR Pfam; PF00282; Pyridoxal_deC; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1. PE 3: Inferred from homology; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382}; KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50, KW ECO:0000256|RuleBase:RU000382}; KW Reference proteome {ECO:0000313|Proteomes:UP000001070}. FT MOD_RES 322 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50" SQ SEQUENCE 510 AA; 57899 MW; 0D19A30F8A53DA49 CRC64; MSLNPNGYKL SERTGKLTAY DLMPTTVTAG AETREFLLKV IDVLLDFVKA TNDRNEKVLD FHHPEDMKRL LDLEVPDRAL PLQQLIEDCA TTLKYQVKTG HPHFFNQLSN GLDLISMAGE WLTATANTNM FTYEIAPVFI LMETVVLTKM REIIGWSGGD SILAPGGSIS NLYAFLAARH KMFPNYKEHG SVGLPGTLVM FTSDQCHYSI KSCAAVCGLG TDHCVMVPSD EHGKMITSEL ERLILERKAK GDIPFFVNAT AGTTVLGAFD DINAIADICQ KYNCWMHVDA AWGGGLLMSR KHRHPRFTGI ERVDSVTWNP HKLMGALFQC STIHFKEDGL LISCNQMSAE YLFMTDKHYD ISYDTGDKVI QCGRHNDIFK LWLQWRAKGT EGFEQQQDRL MELVQYQLKR IREQPDRFHL IMEPECVNVS FWYIPKRLRG VPHDAKKEVE LGKTCPIIKG RMMQKGTLMV GYQPDDRRPN FFRSIISSAA VTEVDVDFML DEIHRLGDDL //