ID A9RR67_PHYPA Unreviewed; 489 AA. AC A9RR67; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Alliinase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM}; GN ORFNames=PHYPA_008116 {ECO:0000313|EMBL:PNR54439.1}; OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta; OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium. OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR54439.1}; RN [1] {ECO:0000313|EMBL:PNR54439.1, ECO:0000313|Proteomes:UP000006727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c5_24670V3.1, RC ECO:0000313|Proteomes:UP000006727}; RX PubMed=18079367; DOI=10.1126/science.1150646; RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H., RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T., RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A., RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y., RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E., RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M., RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J., RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B., RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A., RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y., RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M., RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S., RA Boore J.L.; RT "The Physcomitrella genome reveals evolutionary insights into the conquest RT of land by plants."; RL Science 319:64-69(2008). RN [2] {ECO:0000313|EMBL:PNR54439.1, ECO:0000313|Proteomes:UP000006727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c5_24670V3.1, RC ECO:0000313|Proteomes:UP000006727}; RX PubMed=29237241; DOI=10.1111/tpj.13801; RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B., RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J., RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G., RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W., RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W., RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J., RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M., RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y., RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M., RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J., RA Schmutz J., Rensing S.A.; RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome RT structure and evolution."; RL Plant J. 93:515-533(2018). RN [3] {ECO:0000313|EnsemblPlants:Pp3c5_24670V3.1} RP IDENTIFICATION. RG EnsemblPlants; RL Submitted (DEC-2020) to UniProtKB. CC -!- SIMILARITY: Belongs to the alliinase family. CC {ECO:0000256|ARBA:ARBA00006312}. 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; ABEU02000005; PNR54439.1; -; Genomic_DNA. DR RefSeq; XP_001756693.1; XM_001756641.1. DR AlphaFoldDB; A9RR67; -. DR STRING; 3218.A9RR67; -. DR PaxDb; 3218-PP1S23_275V6-1; -. DR EnsemblPlants; Pp3c5_24670V3.1; Pp3c5_24670V3.1; Pp3c5_24670. DR EnsemblPlants; Pp3c5_24670V3.2; Pp3c5_24670V3.2; Pp3c5_24670. DR EnsemblPlants; Pp3c5_24670V3.3; Pp3c5_24670V3.3; Pp3c5_24670. DR Gramene; Pp3c5_24670V3.1; Pp3c5_24670V3.1; Pp3c5_24670. DR Gramene; Pp3c5_24670V3.2; Pp3c5_24670V3.2; Pp3c5_24670. DR Gramene; Pp3c5_24670V3.3; Pp3c5_24670V3.3; Pp3c5_24670. DR eggNOG; ENOG502QQJV; Eukaryota. DR HOGENOM; CLU_036760_2_0_1; -. DR InParanoid; A9RR67; -. DR OMA; VMSSRWR; -. DR OrthoDB; 1275724at2759; -. DR Proteomes; UP000006727; Chromosome 5. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central. DR GO; GO:0006520; P:amino acid metabolic process; IBA:GO_Central. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 2.10.25.30; EGF-like, alliinase; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR InterPro; IPR006948; Alliinase_C. DR InterPro; IPR037029; Alliinase_N_sf. DR InterPro; IPR006947; EGF_alliinase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR43795:SF110; ALLIINASE_C DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1. DR Pfam; PF04864; Alliinase_C; 1. DR Pfam; PF04863; EGF_alliinase; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|SAM:Phobius}; KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}; KW Reference proteome {ECO:0000313|Proteomes:UP000006727}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 33..53 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 72..125 FT /note="Alliinase EGF-like" FT /evidence="ECO:0000259|Pfam:PF04863" FT DOMAIN 128..485 FT /note="Alliinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF04864" SQ SEQUENCE 489 AA; 53966 MW; D4068418801CE825 CRC64; MEADDTSARL LPLASWQSTH KNSTEAKFSL RNVVLYVSLL VNLPALVIVF HPIQGFLWTP PRSEQPAAPQ WAEAVQAAER AASKWCSGNG NVFVDTVGID ADGSPSCECN DCFAGPDCSL PLPDCVADAI SGDPLLFEAY WRKNSDLGAV VIPAWYRMGY QTRDVTSMPY TEALVASIRE LHAMVGNAVT EGRYIAFGTG STQLINAVIH SLALQDPGRV TPVVSKAPYY NAYYTQTEYF KSPFYSFSGE PDRKVGQQGP AQIEVIASPN NPTTQIQEVP QNVSGHVVYD HAYYWPHLTP ITKAVDYDIM LFTLSKLTGH AGSRIGWVIL KDFDLYTKVL RYADVSTIGL GHEAQLRASQ LIRTIIDGYS EGNSGREGIF HFAHDVLQSR WAKLQAIFQN VSRFSLQELK PGYCSFFKRV SDPSPGYAWI RCNREEDADC SAVLLSAGII GRAGPIFGTT PRYVRLSLLK RASHFDNLAD HLLKLVAQS //