1A1D_PSEUD
ID 1A1D_PSEUD Reviewed; 338 AA.
AC Q00740;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=1-aminocyclopropane-1-carboxylate deaminase {ECO:0000255|HAMAP-Rule:MF_00807};
DE Short=ACC deaminase {ECO:0000255|HAMAP-Rule:MF_00807};
DE Short=ACCD {ECO:0000255|HAMAP-Rule:MF_00807};
DE EC=3.5.99.7 {ECO:0000255|HAMAP-Rule:MF_00807};
GN Name=acdS {ECO:0000255|HAMAP-Rule:MF_00807};
OS Pseudomonas sp. (strain ACP).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=74568;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, AND COFACTOR.
RX PubMed=1885510; DOI=10.1128/jb.173.17.5260-5265.1991;
RA Sheehy R.E., Honma M., Yamada M., Sasaki T., Martineau B., Hiatt W.R.;
RT "Isolation, sequence, and expression in Escherichia coli of the Pseudomonas
RT sp. strain ACP gene encoding 1-aminocyclopropane-1-carboxylate deaminase.";
RL J. Bacteriol. 173:5260-5265(1991).
CC -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the
CC irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to
CC ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen
CC source. {ECO:0000255|HAMAP-Rule:MF_00807, ECO:0000269|PubMed:1885510}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00807,
CC ECO:0000269|PubMed:1885510};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00807,
CC ECO:0000269|PubMed:1885510};
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00807}.
CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC family. {ECO:0000255|HAMAP-Rule:MF_00807}.
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DR EMBL; M73488; AAA25689.1; -; Genomic_DNA.
DR PDB; 1RQX; X-ray; 2.50 A; A/B/C/D=1-338.
DR PDB; 1TYZ; X-ray; 2.00 A; A/B/C/D=1-338.
DR PDB; 1TZ2; X-ray; 2.10 A; A/B/C/D=1-338.
DR PDB; 1TZJ; X-ray; 1.99 A; A/B/C/D=1-338.
DR PDB; 1TZK; X-ray; 2.00 A; A/B/C/D=1-338.
DR PDB; 1TZM; X-ray; 2.08 A; A/B/C/D=1-338.
DR PDBsum; 1RQX; -.
DR PDBsum; 1TYZ; -.
DR PDBsum; 1TZ2; -.
DR PDBsum; 1TZJ; -.
DR PDBsum; 1TZK; -.
DR PDBsum; 1TZM; -.
DR AlphaFoldDB; Q00740; -.
DR SMR; Q00740; -.
DR DrugBank; DB02085; 1-Aminocyclopropanecarboxylic Acid.
DR DrugBank; DB03053; 1-Aminocyclopropylphosphonate.
DR DrugBank; DB01804; 2-Ammoniobut-3-Enoate, 2-Amino-3-Butenoate.
DR DrugBank; DB04212; 2-Iminiopropanoate.
DR DrugBank; DB04553; 2-Oxobutanoic Acid.
DR DrugBank; DB01735; 3-Chloroalaninate.
DR BRENDA; 3.5.99.7; 5085.
DR EvolutionaryTrace; Q00740; -.
DR GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009310; P:amine catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_00807; ACC_deaminase; 1.
DR InterPro; IPR027278; ACCD_DCysDesulf.
DR InterPro; IPR005965; ACP_carboxylate_deaminase.
DR InterPro; IPR020601; ACP_carboxylate_deaminase_bac.
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; Direct protein sequencing; Hydrolase; Pyridoxal phosphate.
FT CHAIN 1..338
FT /note="1-aminocyclopropane-1-carboxylate deaminase"
FT /id="PRO_0000184505"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00807"
FT MOD_RES 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:1TZJ"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1TZJ"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:1TZJ"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:1TZJ"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:1TZJ"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1TZJ"
FT TURN 108..112
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:1TZJ"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 140..150
FT /evidence="ECO:0007829|PDB:1TZJ"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1TZJ"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 171..186
FT /evidence="ECO:0007829|PDB:1TZJ"
FT STRAND 191..200
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:1TZJ"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1TZJ"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 228..246
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:1TZJ"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:1TZJ"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:1TZJ"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 325..331
FT /evidence="ECO:0007829|PDB:1TZJ"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:1TZJ"
SQ SEQUENCE 338 AA; 36672 MW; 01FC286177012FDF CRC64;
MNLQRFPRYP LTFGPTPIQP LARLSKHLGG KVHLYAKRED CNSGLAFGGN KTRKLEYLIP
EALAQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYSDAVY DRVGNIQMSR
ILGADVRLVP DGFDIGFRRS WEDALESVRA AGGKPYAIPA GCSDHPLGGL GFVGFAEEVR
AQEAELGFKF DYVVVCSVTG STQAGMVVGF AADGRADRVI GVDASAKPAQ TREQITRIAR
QTAEKVGLER DIMRADVVLD ERFAGPEYGL PNEGTLEAIR LCARTEGMLT DPVYEGKSMH
GMIEMVRNGE FPEGSRVLYA HLGGVPALNG YSFIFRDG
