GenomeNet

Database: UniProt
Entry: K5XMF0_AGABU
LinkDB: K5XMF0_AGABU
Original site: K5XMF0_AGABU 
ID   K5XMF0_AGABU            Unreviewed;       759 AA.
AC   K5XMF0;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=PABS domain-containing protein {ECO:0000259|PROSITE:PS51006};
GN   ORFNames=AGABI1DRAFT_64147 {ECO:0000313|EMBL:EKM75755.1};
OS   Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS   10392) (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX   NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM75755.1, ECO:0000313|Proteomes:UP000008493};
RN   [1] {ECO:0000313|Proteomes:UP000008493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC   {ECO:0000313|Proteomes:UP000008493};
RX   PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA   Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA   Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA   Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA   Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA   Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA   Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA   Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT   "Genome sequence of the button mushroom Agaricus bisporus reveals
RT   mechanisms governing adaptation to a humic-rich ecological niche.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
CC   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC       {ECO:0000256|ARBA:ARBA00007867, ECO:0000256|RuleBase:RU003836}.
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; JH971409; EKM75755.1; -; Genomic_DNA.
DR   RefSeq; XP_007333601.1; XM_007333539.1.
DR   AlphaFoldDB; K5XMF0; -.
DR   SMR; K5XMF0; -.
DR   STRING; 597362.K5XMF0; -.
DR   GeneID; 18830481; -.
DR   KEGG; abp:AGABI1DRAFT64147; -.
DR   eggNOG; KOG0172; Eukaryota.
DR   eggNOG; KOG1562; Eukaryota.
DR   HOGENOM; CLU_016207_2_0_1; -.
DR   InParanoid; K5XMF0; -.
DR   OMA; PCAEYVV; -.
DR   OrthoDB; 2184985at2759; -.
DR   Proteomes; UP000008493; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 2.30.140.10; Spermidine synthase, tetramerisation domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00198; Spermidine_synth; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR030374; PABS.
DR   InterPro; IPR030373; PABS_CS.
DR   InterPro; IPR032095; Sacchrp_dh-like_C.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR001045; Spermi_synthase.
DR   InterPro; IPR035246; Spermidine_synt_N.
DR   InterPro; IPR037163; Spermidine_synt_N_sf.
DR   NCBIfam; TIGR00417; speE; 1.
DR   PANTHER; PTHR11133:SF25; ALPHA-AMINOADIPIC SEMIALDEHYDE SYNTHASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR   Pfam; PF16653; Sacchrp_dh_C; 1.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   Pfam; PF17284; Spermine_synt_N; 1.
DR   Pfam; PF01564; Spermine_synth; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01330; PABS_1; 1.
DR   PROSITE; PS51006; PABS_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Polyamine biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00354};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008493};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00354}.
FT   DOMAIN          11..246
FT                   /note="PABS"
FT                   /evidence="ECO:0000259|PROSITE:PS51006"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ   SEQUENCE   759 AA;  83634 MW;  591AC5F55BACAD7D CRC64;
     MAPLSHPSIV DGWFREISSQ WPGQAMTLKV NKILHVEKSL YQDVLVFESE TFGNVLVLDG
     VIQCTERDEF SYQEMIAHLP LASHPNPKKV LVVGGGDGGV VREVLKHDTV EQVVLCDIDE
     AVIRVSKQYL PHMSGLLADP RVTVHIGDGF KFLSNNQNTY DVIITDSSDP VGPAESLFQK
     PYFELLHNAL TPGGHISTQG ECQWIQLSLI QDLKRVTTEI FQTTEYAYTT IPTYPSGQIG
     FMVCAKAPGR DLRTPVREVK NTKYYNKDIH RTAFVLPEFT RSVLEEGKDI RPKFGRAAKA
     VEAEAAGRKR KRVLLLGSGF VARPCAEYVV RNPENELTIA CRTLSSAKAL AESLLATTAI
     SLDVNSTDAL EKAIAEHDLV ISLIPYTYHA AVIRAAIKSK THVVTTSYVN PLMRELDAEA
     KAAGIVVFNE IGLDPGIDHL YAVKTINEVH AKGGKIKQFL SFCGGLPAPE CADNPLGYKF
     SWSSRGVLLA LLNTASYISN SQAITVTGAE LMGHAKPYYI SPAFAFVGYP NRDSTPFREW
     YHIPEAETVL RGTLRYQGFP EFIGTLVKLG WLDQTEKEWL KEGITWKQIT KNLVGATAQD
     DLTEAAIVDR INTKVQFSSA SEAERIVSGL RWIGTLSDEP AQIRAGNLLD TLCARLEGLM
     KYEVGERDLV MLQHKFVVEW ADGTTQILTS TLEAYGSTVP GGYSAMALTV GVPCGITVQL
     VLDGVLKEPG VHAPYDYEVC EKIRKVLEIE GLGMVEKVM
//
DBGET integrated database retrieval system