HSS_BLAVI
ID HSS_BLAVI Reviewed; 477 AA.
AC O32323;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Homospermidine synthase;
DE Short=HSS;
DE EC=2.5.1.44;
GN Name=hss;
OS Blastochloris viridis (Rhodopseudomonas viridis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Blastochloridaceae; Blastochloris.
OX NCBI_TaxID=1079;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=DSM 134 / 2450;
RX PubMed=8841401; DOI=10.1111/j.1432-1033.1996.0373h.x;
RA Tholl D., Ober D., Martin W., Kellermann J., Hartmann T.;
RT "Purification, molecular cloning and expression in Escherichia coli of
RT homospermidine synthase from Rhodopseudomonas viridis.";
RL Eur. J. Biochem. 240:373-379(1996).
CC -!- FUNCTION: Involved in the NAD(+)-dependent synthesis of the polyamine
CC homospermidine from putrescine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 putrescine = NH4(+) + sym-homospermidine;
CC Xref=Rhea:RHEA:18645, ChEBI:CHEBI:28938, ChEBI:CHEBI:57811,
CC ChEBI:CHEBI:326268; EC=2.5.1.44;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=putrescine + spermidine = propane-1,3-diamine + sym-
CC homospermidine; Xref=Rhea:RHEA:11236, ChEBI:CHEBI:57484,
CC ChEBI:CHEBI:57811, ChEBI:CHEBI:57834, ChEBI:CHEBI:326268;
CC EC=2.5.1.44;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; L77975; AAB63957.1; -; mRNA.
DR PDB; 4PLP; X-ray; 1.49 A; A/B=1-477.
DR PDB; 4TVB; X-ray; 1.69 A; A/B=1-477.
DR PDB; 4XQ9; X-ray; 1.60 A; A/B=3-476.
DR PDB; 4XQC; X-ray; 1.27 A; A/B=3-477.
DR PDB; 4XQE; X-ray; 1.30 A; A/B=3-476.
DR PDB; 4XQG; X-ray; 1.42 A; A/B=3-477.
DR PDB; 4XR4; X-ray; 1.63 A; A/B=3-476.
DR PDB; 4XRG; X-ray; 1.30 A; A/B=3-476.
DR PDB; 6S3X; X-ray; 1.72 A; A/B=2-477.
DR PDB; 6S49; X-ray; 1.69 A; A/B=2-477.
DR PDB; 6S4D; X-ray; 1.80 A; A/B=2-477.
DR PDB; 6S65; X-ray; 1.75 A; A/B=2-477.
DR PDB; 6S6G; X-ray; 1.60 A; A/B=2-477.
DR PDB; 6S72; X-ray; 1.87 A; A/B=2-477.
DR PDB; 6SEP; X-ray; 2.20 A; A/B=2-477.
DR PDBsum; 4PLP; -.
DR PDBsum; 4TVB; -.
DR PDBsum; 4XQ9; -.
DR PDBsum; 4XQC; -.
DR PDBsum; 4XQE; -.
DR PDBsum; 4XQG; -.
DR PDBsum; 4XR4; -.
DR PDBsum; 4XRG; -.
DR PDBsum; 6S3X; -.
DR PDBsum; 6S49; -.
DR PDBsum; 6S4D; -.
DR PDBsum; 6S65; -.
DR PDBsum; 6S6G; -.
DR PDBsum; 6S72; -.
DR PDBsum; 6SEP; -.
DR AlphaFoldDB; O32323; -.
DR SMR; O32323; -.
DR STRING; 1079.BVIR_716; -.
DR BioCyc; MetaCyc:MON-21190; -.
DR BRENDA; 2.5.1.44; 872.
DR GO; GO:0050514; F:homospermidine synthase (spermidine-specific) activity; IEA:RHEA.
DR GO; GO:0047296; F:homospermidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.360.30; -; 1.
DR InterPro; IPR023181; Homospermid_syn-like_C.
DR InterPro; IPR032095; Sacchrp_dh-like_C.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
DR Pfam; PF16653; Sacchrp_dh_C; 1.
DR Pfam; PF03435; Sacchrp_dh_NADP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; Transferase.
FT CHAIN 1..477
FT /note="Homospermidine synthase"
FT /id="PRO_0000084084"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:6S6G"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6S6G"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:4XQC"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 71..79
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:4XR4"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 135..148
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:4XQC"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 165..180
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 231..239
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:4XQC"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 329..341
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 360..370
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 383..389
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:4PLP"
FT HELIX 395..413
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 427..434
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:4XQC"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:4XQC"
FT TURN 450..453
FT /evidence="ECO:0007829|PDB:4XQC"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:4XQC"
SQ SEQUENCE 477 AA; 52776 MW; 4395065C7F33802C CRC64;
MTDWPVYHRI DGPIVMIGFG SIGRGTLPLI ERHFAFDRSK LVVIDPSDEA RKLAEARGVR
FIQQAVTRDN YRELLVPLLT AGPGQGFCVN LSVDTSSLDI MELARENGAL YIDTVVEPWL
GFYFDPDLKP EARSNYALRE TVLAARRNKP GGTTAVSCCG ANPGMVSWFV KQALVNLAAD
LGVTGEEPTT REEWARLAMD LGVKGIHIAE RDTQRASFPK PFDVFVNTWS VEGFVSEGLQ
PAELGWGTFE RWMPDNARGH DSGCGAGIYL LQPGANTRVR SWTPTAMAQY GFLVTHNESI
SIADFLTVRD AAGQAVYRPT CHYAYHPCND AVLSLHEMFG SGKRQSDWRI LDETEIVDGI
DELGVLLYGH GKNAYWYGSQ LSIEETRRIA PDQNATGLQV SSAVLAGMVW ALENPNAGIV
EADDLDFRRC LEVQTPYLGP VVGVYTDWTP LAGRPGLFPE DIDTSDPWQF RNVLVRD
