ATXA_STRGL
ID ATXA_STRGL Reviewed; 143 AA.
AC P01551;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Actinoxanthin;
DE Short=AXN;
DE Flags: Precursor;
GN Name=axnA;
OS Streptomyces globisporus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1908;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8226326; DOI=10.7164/antibiotics.46.1475;
RA Sakata N., Mase S., Ikeno S., Hori M., Otani T.;
RT "The amino acid sequence of actinoxanthin apoprotein deduced from the base
RT sequence of the gene.";
RL J. Antibiot. 46:1475-1477(1993).
RN [2]
RP PROTEIN SEQUENCE OF 34-143.
RX PubMed=994323; DOI=10.7164/antibiotics.29.1026;
RA Khokhlov A.S., Reshetov P.D., Chupova L.A., Cherches B.Z., Zhigis L.S.,
RA Stoyachenko I.A.;
RT "Chemical studies on actinoxanthin.";
RL Jpn. J. Antibiot. 29:1026-1034(1976).
RN [3]
RP DISULFIDE BONDS.
RA Zhigis L.S., Stoyachenko I.A., Cherches B.Z., Reshetov P.D., Khokhlov A.S.;
RT "Actinoxanthin. VII. Location of disulfide bonds.";
RL Bioorg. Khim. 2:506-510(1976).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS).
RA Pletnev V.Z., Kuzin A.P., Trakhanov S.D., Kostetsky P.V., Popovich V.A.,
RA Tsigannik I.N.;
RT "Three-dimensional structure of actinoxanthin. III. A 4-A resolution.";
RL Biopolymers 20:679-694(1981).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RA Pletnev V.Z., Kuzin A.P., Trakhanov S.D., Kostetsky P.V.;
RT "Three-dimensional structure of actinoxanthin. IV. A 2.5-A resolution.";
RL Biopolymers 21:287-300(1982).
CC -!- FUNCTION: Binds non-covalently to a chromophore which is the cytotoxic
CC and mutagenic component of the antibiotic. The chromophore binds to DNA
CC as a weak intercalator and causes single- and double-strand breaks.
CC -!- SIMILARITY: Belongs to the neocarzinostatin family. {ECO:0000305}.
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DR EMBL; D11457; BAA02014.1; -; Genomic_DNA.
DR PDB; 1ACX; X-ray; 2.00 A; A=34-143.
DR PDBsum; 1ACX; -.
DR AlphaFoldDB; P01551; -.
DR BMRB; P01551; -.
DR SMR; P01551; -.
DR EvolutionaryTrace; P01551; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR027273; Neocarzinostatin-like.
DR InterPro; IPR002186; Neocarzinostatin_fam.
DR Pfam; PF00960; Neocarzinostat; 1.
DR PRINTS; PR01885; MACROMOMYCIN.
DR SUPFAM; SSF49319; SSF49319; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; DNA-binding; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:994323"
FT CHAIN 34..143
FT /note="Actinoxanthin"
FT /id="PRO_0000019458"
FT DISULFID 69..78
FT /evidence="ECO:0000269|Ref.3"
FT DISULFID 119..124
FT /evidence="ECO:0000269|Ref.3"
FT CONFLICT 54..55
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="S -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="E -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:1ACX"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:1ACX"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:1ACX"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1ACX"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1ACX"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1ACX"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1ACX"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:1ACX"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:1ACX"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:1ACX"
SQ SEQUENCE 143 AA; 13887 MW; 2CB2E57FA5DC2F2C CRC64;
MSLRHMSRRA SRFGVVAVAS IGLAAAAQSV AFAAPAFSVS PASGLSDGQS VSVSVSGAAA
GETYYIAQCA PVGGQDACNP ATATSFTTDA SGAASFSFVV RKSYAGSTPE GTPVGSVDCA
TDACNLGAGN SGLDLGHVAL TFG