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BPSA_THEKO
ID   BPSA_THEKO              Reviewed;         351 AA.
AC   Q5JIZ3;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=N(4)-bis(aminopropyl)spermidine synthase {ECO:0000255|HAMAP-Rule:MF_01947, ECO:0000305};
DE            EC=2.5.1.128 {ECO:0000255|HAMAP-Rule:MF_01947, ECO:0000269|PubMed:24610711};
DE   AltName: Full=Branched-chain polyamine synthase A {ECO:0000255|HAMAP-Rule:MF_01947, ECO:0000303|PubMed:24610711};
GN   Name=bpsA {ECO:0000255|HAMAP-Rule:MF_01947, ECO:0000303|PubMed:24610711};
GN   OrderedLocusNames=TK1691 {ECO:0000312|EMBL:BAD85880.1};
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=24610711; DOI=10.1128/jb.01515-14;
RA   Okada K., Hidese R., Fukuda W., Niitsu M., Takao K., Horai Y., Umezawa N.,
RA   Higuchi T., Oshima T., Yoshikawa Y., Imanaka T., Fujiwara S.;
RT   "Identification of a novel aminopropyltransferase involved in the synthesis
RT   of branched-chain polyamines in hyperthermophiles.";
RL   J. Bacteriol. 196:1866-1876(2014).
CC   -!- FUNCTION: Involved in the biosynthesis of branched-chain polyamines,
CC       which support the growth of thermophiles under high-temperature
CC       conditions. Catalyzes the sequential condensation of spermidine with
CC       the aminopropyl groups of decarboxylated S-adenosylmethionines to
CC       produce N(4)-bis(aminopropyl)spermidine via N(4)-aminopropylspermidine.
CC       Can also use spermine to produce N(4)-aminopropylspermine.
CC       {ECO:0000269|PubMed:24610711}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = 2
CC         H(+) + N(4)-bis(aminopropyl)spermidine + 2 S-methyl-5'-thioadenosine;
CC         Xref=Rhea:RHEA:44132, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC         ChEBI:CHEBI:57443, ChEBI:CHEBI:57834, ChEBI:CHEBI:82771;
CC         EC=2.5.1.128; Evidence={ECO:0000255|HAMAP-Rule:MF_01947,
CC         ECO:0000269|PubMed:24610711};
CC   -!- PATHWAY: Amine and polyamine biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_01947, ECO:0000269|PubMed:24610711}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01947,
CC       ECO:0000269|PubMed:24610711}.
CC   -!- DISRUPTION PHENOTYPE: Grows at 85 degrees Celsius with a slightly
CC       longer lag phase, but is unable to grow at 93 degrees Celsius.
CC       {ECO:0000269|PubMed:24610711}.
CC   -!- SIMILARITY: Belongs to the branched-chain polyamine synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01947, ECO:0000305}.
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DR   EMBL; AP006878; BAD85880.1; -; Genomic_DNA.
DR   RefSeq; WP_011250642.1; NC_006624.1.
DR   PDB; 5XNC; X-ray; 1.84 A; A/B/C/D/E/F/G=1-351.
DR   PDB; 5XNF; X-ray; 1.90 A; A/B=1-351.
DR   PDB; 5XNH; X-ray; 1.95 A; A/H=1-351.
DR   PDB; 6J26; X-ray; 2.00 A; A/B=1-351.
DR   PDBsum; 5XNC; -.
DR   PDBsum; 5XNF; -.
DR   PDBsum; 5XNH; -.
DR   PDBsum; 6J26; -.
DR   AlphaFoldDB; Q5JIZ3; -.
DR   SMR; Q5JIZ3; -.
DR   STRING; 69014.TK1691; -.
DR   EnsemblBacteria; BAD85880; BAD85880; TK1691.
DR   GeneID; 3234997; -.
DR   KEGG; tko:TK1691; -.
DR   PATRIC; fig|69014.16.peg.1649; -.
DR   eggNOG; arCOG00913; Archaea.
DR   HOGENOM; CLU_042160_0_0_2; -.
DR   InParanoid; Q5JIZ3; -.
DR   OMA; KSYMFRI; -.
DR   OrthoDB; 23573at2157; -.
DR   PhylomeDB; Q5JIZ3; -.
DR   BioCyc; MetaCyc:MON-21054; -.
DR   BRENDA; 2.5.1.128; 5246.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IBA:GO_Central.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:UniProtKB.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01947; Aminopropyltransf_BpsA; 1.
DR   InterPro; IPR014435; BpsA.
DR   InterPro; IPR002723; BpsA_C.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF01861; DUF43; 1.
DR   PIRSF; PIRSF005895; UCP005895_mtase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Polyamine biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..351
FT                   /note="N(4)-bis(aminopropyl)spermidine synthase"
FT                   /id="PRO_0000432214"
FT   HELIX           1..9
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           18..30
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           34..41
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           45..57
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   STRAND          60..64
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   STRAND          67..70
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           72..81
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   TURN            92..96
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           102..104
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           105..114
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           123..125
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           132..144
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   STRAND          152..156
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           162..169
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   STRAND          173..180
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           182..195
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   STRAND          199..204
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           213..215
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   STRAND          219..224
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           230..243
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   STRAND          250..255
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   STRAND          257..259
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           262..274
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   STRAND          279..290
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           296..298
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           300..304
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   STRAND          317..324
FT                   /evidence="ECO:0007829|PDB:5XNC"
FT   HELIX           340..342
FT                   /evidence="ECO:0007829|PDB:5XNC"
SQ   SEQUENCE   351 AA;  40229 MW;  06FC2F12957B4568 CRC64;
     MREIIERVKE KTTIPVYERT IENVLSAIQA SGDVWRIVDL SEEPLPLVVA VVTALYELGY
     VAFENNQVIL TRKGKELVEK YGIGPRADYT CSHCQGRTVE IDAFSELLEQ FKEITRDRPE
     PAHQFDQAYV TPETTVARVA LMHSRGDLEN KEVFVLGDDD LTSVALMLSG LPKRIAVLDI
     DERLTKFIEK AADEIGYENI EIFTFDLRKP LPDYALHKFD TFITDPPETV EAIRAFVGRG
     IATLKGPGCA GYFGITRRES SLDKWREIQR VLLNEFGVVI TDIIRNFNEY VNWGYVEETR
     AWRLLPIKVK PSYNWYKSYM FRIQTLEGSK GFEDEITVGQ ELYDDEESST T
 
 
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