1A1D_CYBSA
ID 1A1D_CYBSA Reviewed; 341 AA.
AC Q7M523;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=1-aminocyclopropane-1-carboxylate deaminase;
DE Short=ACC deaminase;
DE Short=ACCD;
DE EC=3.5.99.7;
OS Cyberlindnera saturnus (Yeast) (Williopsis saturnus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=907340;
RN [1]
RP NUCLEOTIDE SEQUENCE, CHARACTERIZATION, AND ACETYLATION AT SER-1.
RX PubMed=9604000; DOI=10.1093/oxfordjournals.jbchem.a022050;
RA Minami R., Uchiyama K., Murakami T., Kawai J., Mikami K., Yamada T.,
RA Yokoi D., Ito H., Matsui H., Honma M.;
RT "Properties, sequence, and synthesis in Escherichia coli of 1-
RT aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus.";
RL J. Biochem. 123:1112-1118(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10938279; DOI=10.1074/jbc.m004681200;
RA Yao M., Ose T., Sugimoto H., Horiuchi A., Nakagawa A., Wakatsuki S.,
RA Yokoi D., Murakami T., Honma M., Tanaka I.;
RT "Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from
RT Hansenula saturnus.";
RL J. Biol. Chem. 275:34557-34565(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).
RX PubMed=12882962; DOI=10.1074/jbc.m305865200;
RA Ose T., Fujino A., Yao M., Watanabe N., Honma M., Tanaka I.;
RT "Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate
RT deaminase: insight into PLP-dependent cyclopropane ring-opening reaction.";
RL J. Biol. Chem. 278:41069-41076(2003).
CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the
CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to
CC ammonia and alpha-ketobutyrate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate +
CC NH4(+); Xref=Rhea:RHEA:16933, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58360; EC=3.5.99.7;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC family. {ECO:0000305}.
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DR PIR; PW0041; PW0041.
DR PDB; 1F2D; X-ray; 2.00 A; A/B/C/D=2-341.
DR PDB; 1J0C; X-ray; 2.75 A; A/B/C/D=1-341.
DR PDB; 1J0D; X-ray; 2.20 A; A/B/C/D=1-341.
DR PDB; 1J0E; X-ray; 2.45 A; A/B/C/D=1-341.
DR PDBsum; 1F2D; -.
DR PDBsum; 1J0C; -.
DR PDBsum; 1J0D; -.
DR PDBsum; 1J0E; -.
DR AlphaFoldDB; Q7M523; -.
DR SMR; Q7M523; -.
DR iPTMnet; Q7M523; -.
DR BRENDA; 3.5.99.7; 2588.
DR EvolutionaryTrace; Q7M523; -.
DR GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009310; P:amine catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR005965; ACP_carboxylate_deaminase.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR PANTHER; PTHR43780; PTHR43780; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR01274; ACC_deam; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Hydrolase; Pyridoxal phosphate.
FT CHAIN 1..341
FT /note="1-aminocyclopropane-1-carboxylate deaminase"
FT /id="PRO_0000184512"
FT ACT_SITE 78
FT /note="Nucleophile"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9604000"
FT MOD_RES 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT TURN 2..4
FT /evidence="ECO:0007829|PDB:1J0C"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1F2D"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:1F2D"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1F2D"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:1F2D"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:1F2D"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:1F2D"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1F2D"
FT TURN 110..115
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:1F2D"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:1F2D"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1F2D"
FT TURN 169..173
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 174..189
FT /evidence="ECO:0007829|PDB:1F2D"
FT STRAND 194..203
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1F2D"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 231..249
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:1F2D"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:1F2D"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:1F2D"
FT HELIX 326..335
FT /evidence="ECO:0007829|PDB:1F2D"
SQ SEQUENCE 341 AA; 37061 MW; 64904CDD7AA2C5FA CRC64;
SGVAKFAKYP LTFGPSPISN LNRLSQHLGS KVNVYAKRED CNSGLAFGGN KLRKLEYIVP
DIVEGDYTHL VSIGGRQSNQ TRMVAALAAK LGKKCVLIQE DWVPIPEAEK DVYNRVGNIE
LSRIMGADVR VIEDGFDIGM RKSFANALQE LEDAGHKPYP IPAGCSEHKY GGLGFVGFAD
EVINQEVELG IKFDKIVVCC VTGSTTAGIL AGMAQYGRQD DVIAIDASFT SEKTKEQTLR
IANNTAKLIG VEHEFKDFTL DTRFAYPCYG VPNEGTIEAI RTCAEQEGVL TDPVYEGKSM
QGLIALIKED YFKPGANVLY VHLGGAPALS AYSSFFPTKT A
